HSP90 is a highly conserved and essential stress protein that is expressed in all eukaryotic cells. From a functional perspective, HSP90 participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex (1-4). Despite its label of being a heat-shock protein, HSP90 is one of the most highly expressed proteins in unstressed cells (12% of cytosolic protein). It carries out a number of housekeeping functions including controlling the activity, turnover, and trafficking of a variety of proteins. Most of the HSP90-regulated proteins that have been discovered to date are involved in cell signaling (5-6). The number of proteins now know to interact with HSP90 is about 100. Target proteins include the kinases v-Src, Wee1, and c-Raf, transcriptional regulators such as p53 and steroid receptors, and the polymerases of the hepatitis B virus and telomerase.5. When bound to ATP, HSP90 interacts with co-chaperones Cdc37, p23, and an assortment of immunophilin-like proteins, forming a complex that stabilizes and protects target proteins from proteasomal degradation. In most cases, HSP90-interacting proteins have been shown to co-precipitate with HSP90 when carrying out immunoadsorption studies, and to exist in cytosolic heterocomplexes with it. In a number of cases, variations in HSP90 expression or HSP90 mutation has been shown to degrade signaling function via the protein or to impair a specific function of the protein (such as steroid binding, kinase activity) in vivo. Ansamycin antibiotics, such as geldanamycin and radicicol, inhibit HSP90 function (7). Looking for more information on HSP90? Visit our new HSP90 Scientific Resource Guide at http://www.HSP90.ca.
HSP90 is a highly conserved and essential stress protein that is expressed in all eukaryotic cells. From a functional perspective, HSP90 participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex (1-4). Despite its label of being a heat-shock protein, HSP90 is one of the most highly expressed proteins in unstressed cells (12% of cytosolic protein). It carries out a number of housekeeping functions including controlling the activity, turnover, and trafficking of a variety of proteins. Most of the HSP90-regulated proteins that have been discovered to date are involved in cell signaling (5-6). The number of proteins now know to interact with HSP90 is about 100. Target proteins include the kinases v-Src, Wee1, and c-Raf, transcriptional regulators such as p53 and steroid receptors, and the polymerases of the hepatitis B virus and telomerase.5. When bound to ATP, HSP90 interacts with co-chaperones Cdc37, p23, and an assortment of immunophilin-like proteins, forming a complex that stabilizes and protects target proteins from proteasomal degradation. In most cases, HSP90-interacting proteins have been shown to co-precipitate with HSP90 when carrying out immunoadsorption studies, and to exist in cytosolic heterocomplexes with it. In a number of cases, variations in HSP90 expression or HSP90 mutation has been shown to degrade signaling function via the protein or to impair a specific function of the protein (such as steroid binding, kinase activity) in vivo. Ansamycin antibiotics, such as geldanamycin and radicicol, inhibit HSP90 function (7). Looking for more information on HSP90? Visit our new HSP90 Scientific Resource Guide at http://www.HSP90.ca.
HSP90 is a highly conserved and essential stress protein that is expressed in all eukaryotic cells. From a functional perspective, HSP90 participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex (1-4). Despite its label of being a heat-shock protein, HSP90 is one of the most highly expressed proteins in unstressed cells (12% of cytosolic protein). It carries out a number of housekeeping functions including controlling the activity, turnover, and trafficking of a variety of proteins. Most of the HSP90-regulated proteins that have been discovered to date are involved in cell signaling (5-6). The number of proteins now know to interact with HSP90 is about 100. Target proteins include the kinases v-Src, Wee1, and c-Raf, transcriptional regulators such as p53 and steroid receptors, and the polymerases of the hepatitis B virus and telomerase.5. When bound to ATP, HSP90 interacts with co-chaperones Cdc37, p23, and an assortment of immunophilin-like proteins, forming a complex that stabilizes and protects target proteins from proteasomal degradation. In most cases, HSP90-interacting proteins have been shown to co-precipitate with HSP90 when carrying out immunoadsorption studies, and to exist in cytosolic heterocomplexes with it. In a number of cases, variations in HSP90 expression or HSP90 mutation has been shown to degrade signaling function via the protein or to impair a specific function of the protein (such as steroid binding, kinase activity) in vivo. Ansamycin antibiotics, such as geldanamycin and radicicol, inhibit HSP90 function (7). Looking for more information on HSP90? Visit our new HSP90 Scientific Resource Guide at http://www.HSP90.ca.
HSP90 is a highly conserved and essential stress protein that is expressed in all eukaryotic cells. From a functional perspective, HSP90 participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex (1-4). Despite its label of being a heat-shock protein, HSP90 is one of the most highly expressed proteins in unstressed cells (12% of cytosolic protein). It carries out a number of housekeeping functions including controlling the activity, turnover, and trafficking of a variety of proteins. Most of the HSP90-regulated proteins that have been discovered to date are involved in cell signaling (5-6). The number of proteins now know to interact with HSP90 is about 100. Target proteins include the kinases v-Src, Wee1, and c-Raf, transcriptional regulators such as p53 and steroid receptors, and the polymerases of the hepatitis B virus and telomerase.5. When bound to ATP, HSP90 interacts with co-chaperones Cdc37, p23, and an assortment of immunophilin-like proteins, forming a complex that stabilizes and protects target proteins from proteasomal degradation. In most cases, HSP90-interacting proteins have been shown to co-precipitate with HSP90 when carrying out immunoadsorption studies, and to exist in cytosolic heterocomplexes with it. In a number of cases, variations in HSP90 expression or HSP90 mutation has been shown to degrade signaling function via the protein or to impair a specific function of the protein (such as steroid binding, kinase activity) in vivo. Ansamycin antibiotics, such as geldanamycin and radicicol, inhibit HSP90 function (7). Looking for more information on HSP90? Visit our new HSP90 Scientific Resource Guide at http://www.HSP90.ca.
Product Type:
Protein
Format:
20mM Tris, pH7.5, 175 mM NaCl, 0.1 mM EDTA, 10% glycerol, 1 mM DTT
Storage Temp:
-20ºC
Applications:
WB | SDS-PAGE | Functional Assay | ELISA | Co-IP
Target:
HSP90 beta
Conjugate:
No tag
Research Area(s):
Cancer | Heat Shock | Cell Signaling | Protein Trafficking | Chaperone Proteins | Cancer | Tumor Biomarkers
HSP90 is a highly conserved and essential stress protein that is expressed in all eukaryotic cells. From a functional perspective, HSP90 participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex (1-4). Despite its label of being a heat-shock protein, HSP90 is one of the most highly expressed proteins in unstressed cells (12% of cytosolic protein). It carries out a number of housekeeping functions including controlling the activity, turnover, and trafficking of a variety of proteins. Most of the HSP90-regulated proteins that have been discovered to date are involved in cell signaling (5-6). The number of proteins now know to interact with HSP90 is about 100. Target proteins include the kinases v-Src, Wee1, and c-Raf, transcriptional regulators such as p53 and steroid receptors, and the polymerases of the hepatitis B virus and telomerase.5. When bound to ATP, HSP90 interacts with co-chaperones Cdc37, p23, and an assortment of immunophilin-like proteins, forming a complex that stabilizes and protects target proteins from proteasomal degradation. In most cases, HSP90-interacting proteins have been shown to co-precipitate with HSP90 when carrying out immunoadsorption studies, and to exist in cytosolic heterocomplexes with it. In a number of cases, variations in HSP90 expression or HSP90 mutation has been shown to degrade signaling function via the protein or to impair a specific function of the protein (such as steroid binding, kinase activity) in vivo. Ansamycin antibiotics, such as geldanamycin and radicicol, inhibit HSP90 function (7). Looking for more information on HSP90? Visit our new HSP90 Scientific Resource Guide at http://www.HSP90.ca.
Product Type:
Protein
Format:
20mM Tris, pH7.5, 175 mM NaCl, 0.1 mM EDTA, 10% glycerol, 1 mM DTT
Storage Temp:
-20ºC
Applications:
WB | SDS-PAGE | Functional Assay | ELISA | Co-IP
Target:
HSP90 beta
Conjugate:
No tag
Research Area(s):
Cancer | Heat Shock | Cell Signaling | Protein Trafficking | Chaperone Proteins | Cancer | Tumor Biomarkers
HSP90 is a highly conserved and essential stress protein that is expressed in all eukaryotic cells. From a functional perspective, HSP90 participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex (1-4). Despite its label of being a heat-shock protein, HSP90 is one of the most highly expressed proteins in unstressed cells (12% of cytosolic protein). It carries out a number of housekeeping functions including controlling the activity, turnover, and trafficking of a variety of proteins. Most of the HSP90-regulated proteins that have been discovered to date are involved in cell signaling (5-6). The number of proteins now know to interact with HSP90 is about 100. Target proteins include the kinases v-Src, Wee1, and c-Raf, transcriptional regulators such as p53 and steroid receptors, and the polymerases of the hepatitis B virus and telomerase.5. When bound to ATP, HSP90 interacts with co-chaperones Cdc37, p23, and an assortment of immunophilin-like proteins, forming a complex that stabilizes and protects target proteins from proteasomal degradation. In most cases, HSP90-interacting proteins have been shown to co-precipitate with HSP90 when carrying out immunoadsorption studies, and to exist in cytosolic heterocomplexes with it. In a number of cases, variations in HSP90 expression or HSP90 mutation has been shown to degrade signaling function via the protein or to impair a specific function of the protein (such as steroid binding, kinase activity) in vivo. Ansamycin antibiotics, such as geldanamycin and radicicol, inhibit HSP90 function (7). Looking for more information on HSP90? Visit our new HSP90 Scientific Resource Guide at http://www.HSP90.ca.
Product Type:
Protein
Format:
20mM Tris, pH7.5, 175 mM NaCl, 0.1 mM EDTA, 10% glycerol, 1 mM DTT
Storage Temp:
-20ºC
Applications:
WB | SDS-PAGE | Functional Assay | ELISA | Co-IP
Target:
HSP90 beta
Conjugate:
No tag
Research Area(s):
Cancer | Heat Shock | Cell Signaling | Protein Trafficking | Chaperone Proteins | Cancer | Tumor Biomarkers
HSP70 genes encode abundant heat-inducible 70-kDa HSPs (HSP70s). In most eukaryotes HSP70 genes exist as part of a multigene family. They are found in most cellular compartments of eukaryotes including nuclei, mitochondria, chloroplasts, the endoplasmic reticulum and the cytosol, as well as in bacteria. The genes show a high degree of conservation, having at least 50% identity (2). The N-terminal two thirds of HSP70s are more conserved than the C-terminal third. HSP70 binds ATP with high affinity and possesses a weak ATPase activity which can be stimulated by binding to unfolded proteins and synthetic peptides (3). When HSC70 (constitutively expressed) present in mammalian cells was truncated, ATP binding activity was found to reside in an N-terminal fragment of 44kDa which lacked peptide binding capacity. Polypeptide binding ability therefore resided within the C-terminal half (4). The structure of this ATP binding domain displays multiple features of nucleotide binding proteins (5). All HSP70s, regardless of location, bind proteins, particularly unfolded ones. The molecular chaperones of the HSP70 family recognize and bind to nascent polypeptide chains as well as partially folded intermediates of proteins preventing their aggregation and misfolding. The binding of ATP triggers a critical conformational change leading to the release of the bound substrate protein (6). The universal ability of HSP70s to undergo cycles of binding to and release from hydrophobic stretches of partially unfolded proteins determines their role in a great variety of vital intracellular functions such as protein synthesis, protein folding and oligomerization and protein transport. Looking for more information on HSP70? Visit our new HSP70 Scientific Resource Guide at http://www.HSP70.com.
This product has been certified >90% pure using SDS-PAGE analysis. The protein has ATPase activity at the time of manufacture of 3.3µM phosphate liberated/hr/µg protein in a 200µl reaction at 37°C (pH7.5) in the presence of 20ul of 1mM ATP using a Malachite Green assay.
Cellular Localization:
Cytoplasm
References:
1. Zho J. (1998) Cell. 94: 471-480. 2. Boorstein, W. R., Ziegelhoffer, T. & Craig, E. A. (1993) J. Mol. Evol. 38(1): 1-17. 3. Rothman J. (1989) Cell. 59: 591 -601. 4. DeLuca-Flaherty et al. (1990) Cell. 62: 875-887. 5. Bork P., Sander C. & Valencia A. (1992) Proc. Natl Acad. Sci. USA. 89: 7290-7294. 6. Fink A.L. (1999) Physiol. Rev. 79: 425-449. 7. Smith D.F., et al., (1993) Mol. Cell. Biol. 13(2): 869-876. 8. Prapapanich V., et al., (1996) Mol. Cell. Biol. 16(11): 6200-6207. 9. Fernandez-Funez et al., (2000) Nature. 408(6808): 101-106.
HSP70 genes encode abundant heat-inducible 70-kDa HSPs (HSP70s). In most eukaryotes HSP70 genes exist as part of a multigene family. They are found in most cellular compartments of eukaryotes including nuclei, mitochondria, chloroplasts, the endoplasmic reticulum and the cytosol, as well as in bacteria. The genes show a high degree of conservation, having at least 50% identity (2). The N-terminal two thirds of HSP70s are more conserved than the C-terminal third. HSP70 binds ATP with high affinity and possesses a weak ATPase activity which can be stimulated by binding to unfolded proteins and synthetic peptides (3). When HSC70 (constitutively expressed) present in mammalian cells was truncated, ATP binding activity was found to reside in an N-terminal fragment of 44kDa which lacked peptide binding capacity. Polypeptide binding ability therefore resided within the C-terminal half (4). The structure of this ATP binding domain displays multiple features of nucleotide binding proteins (5). All HSP70s, regardless of location, bind proteins, particularly unfolded ones. The molecular chaperones of the HSP70 family recognize and bind to nascent polypeptide chains as well as partially folded intermediates of proteins preventing their aggregation and misfolding. The binding of ATP triggers a critical conformational change leading to the release of the bound substrate protein (6). The universal ability of HSP70s to undergo cycles of binding to and release from hydrophobic stretches of partially unfolded proteins determines their role in a great variety of vital intracellular functions such as protein synthesis, protein folding and oligomerization and protein transport. Looking for more information on HSP70? Visit our new HSP70 Scientific Resource Guide at http://www.HSP70.com.
This product has been certified >90% pure using SDS-PAGE analysis. The protein has ATPase activity at the time of manufacture of 3.3µM phosphate liberated/hr/µg protein in a 200µl reaction at 37°C (pH7.5) in the presence of 20ul of 1mM ATP using a Malachite Green assay.
Cellular Localization:
Cytoplasm
References:
1. Zho J. (1998) Cell. 94: 471-480. 2. Boorstein, W. R., Ziegelhoffer, T. & Craig, E. A. (1993) J. Mol. Evol. 38(1): 1-17. 3. Rothman J. (1989) Cell. 59: 591 -601. 4. DeLuca-Flaherty et al. (1990) Cell. 62: 875-887. 5. Bork P., Sander C. & Valencia A. (1992) Proc. Natl Acad. Sci. USA. 89: 7290-7294. 6. Fink A.L. (1999) Physiol. Rev. 79: 425-449. 7. Smith D.F., et al., (1993) Mol. Cell. Biol. 13(2): 869-876. 8. Prapapanich V., et al., (1996) Mol. Cell. Biol. 16(11): 6200-6207. 9. Fernandez-Funez et al., (2000) Nature. 408(6808): 101-106.
HSP70 genes encode abundant heat-inducible 70-kDa HSPs (HSP70s). In most eukaryotes HSP70 genes exist as part of a multigene family. They are found in most cellular compartments of eukaryotes including nuclei, mitochondria, chloroplasts, the endoplasmic reticulum and the cytosol, as well as in bacteria. The genes show a high degree of conservation, having at least 50% identity (2). The N-terminal two thirds of HSP70s are more conserved than the C-terminal third. HSP70 binds ATP with high affinity and possesses a weak ATPase activity which can be stimulated by binding to unfolded proteins and synthetic peptides (3). When HSC70 (constitutively expressed) present in mammalian cells was truncated, ATP binding activity was found to reside in an N-terminal fragment of 44kDa which lacked peptide binding capacity. Polypeptide binding ability therefore resided within the C-terminal half (4). The structure of this ATP binding domain displays multiple features of nucleotide binding proteins (5). All HSP70s, regardless of location, bind proteins, particularly unfolded ones. The molecular chaperones of the HSP70 family recognize and bind to nascent polypeptide chains as well as partially folded intermediates of proteins preventing their aggregation and misfolding. The binding of ATP triggers a critical conformational change leading to the release of the bound substrate protein (6). The universal ability of HSP70s to undergo cycles of binding to and release from hydrophobic stretches of partially unfolded proteins determines their role in a great variety of vital intracellular functions such as protein synthesis, protein folding and oligomerization and protein transport. Looking for more information on HSP70? Visit our new HSP70 Scientific Resource Guide at http://www.HSP70.com.
This product has been certified >90% pure using SDS-PAGE analysis. The protein has ATPase activity at the time of manufacture of 3.3µM phosphate liberated/hr/µg protein in a 200µl reaction at 37°C (pH7.5) in the presence of 20ul of 1mM ATP using a Malachite Green assay.
Cellular Localization:
Cytoplasm
References:
1. Zho J. (1998) Cell. 94: 471-480. 2. Boorstein, W. R., Ziegelhoffer, T. & Craig, E. A. (1993) J. Mol. Evol. 38(1): 1-17. 3. Rothman J. (1989) Cell. 59: 591 -601. 4. DeLuca-Flaherty et al. (1990) Cell. 62: 875-887. 5. Bork P., Sander C. & Valencia A. (1992) Proc. Natl Acad. Sci. USA. 89: 7290-7294. 6. Fink A.L. (1999) Physiol. Rev. 79: 425-449. 7. Smith D.F., et al., (1993) Mol. Cell. Biol. 13(2): 869-876. 8. Prapapanich V., et al., (1996) Mol. Cell. Biol. 16(11): 6200-6207. 9. Fernandez-Funez et al., (2000) Nature. 408(6808): 101-106.
In both prokaryotic and eukaryotic cells, the misfolding and aggregation of proteins during biogenesis and under conditions of cellular stress are prevented by molecular chaperones. Members of the HSP60 family of heat shock proteins are some of the best characterized chaperones. HSP60, also known as Cpn60 or GroEl, is an abundant protein synthesized constitutively in the cell that is induced to a higher concentration after brief cell shock. It is present in many species and exhibits a remarkable sequence homology among various counterparts in bacteria, plants, and mammals with more than half of the residues identical between bacterial and mammalian HSP60 (1-3). Whereas mammalian HSP60 is localized within the mitochondria, plant HSP60, or otherwise known as Rubisco-binding protein, is located in plant chloroplasts. It has been indicated that these proteins carry out a very important biological function due to the fact that HSP60 is present in so many different species. The common characteristics of the HSP60s from the divergent species are i) high abundance, ii) induction with environmental stress such as heat shock, iii) homo-oligomeric structures of either 7 or 14 subunits which reversibly dissociate in the presence of Mg2+ and ATP, iv) ATPase activity and v) a role in folding and assembly of oligomeric protein structures (4). These similarities are supported by recent studies where the single-ring human mitochondrial homolog, HSP60 with its co-chaperonin, HSP10 were expressed in a E. coli strain, engineered so that the groE operon is under strict regulatory control. This study has demonstrated that expression of HSP60-HSP10 was able to carry out all essential in vivo functions of GroEL and its co-chaperonin, GroES (5). Another important function of HSP60 and HSP10 is their protective functions against infection and cellular stress. HSP60 has however been linked to a number of autoimmune diseases, as well as Alzheimer's, coronary artery diseases, MS, and diabetes (6-9).
This product has been certified >90% pure using SDS-PAGE analysis. The protein has ATPase activity at the time of manufacture of 3.6µM phosphate liberated/hr/µg protein in a 200µl reaction at 37°C (pH7.5) in the presence of 20ul of 1mM ATP using a Malachite Green assay.
Cellular Localization:
Mitochondrion Matrix
References:
1. Hartl F.U. (1996) Nature. 381: 571-579. 2. Bukau B. and Horwich A.L. (1998) Cell. 92: 351-366. 3.Hartl F.U. and Hayer-Hartl M. (2002) Science. 295: 1852-1858. 4. Jindal S., et al. (1989) Molecular and Cellular Biol. 9: 2279-2283. 5. La Verda D., et al (1999) Infect Dis. Obstet. Gynecol. 7: 64-71. 6. Itoh H., et al. (2002) Eur. J. Biochem. 269: 5931-5938. 7.Gupta S. and Knowlton A.A. J. Cell Mol Med. 9: 51-58. 8. Deocaris C.C. et al. (2006) Cell Stress Chaperones. 11: 116-128. 9. Lai H.C., et al. (2007) Am. J. Physiol. Endocrinol. Metab. 292: E292-E297.
In both prokaryotic and eukaryotic cells, the misfolding and aggregation of proteins during biogenesis and under conditions of cellular stress are prevented by molecular chaperones. Members of the HSP60 family of heat shock proteins are some of the best characterized chaperones. HSP60, also known as Cpn60 or GroEl, is an abundant protein synthesized constitutively in the cell that is induced to a higher concentration after brief cell shock. It is present in many species and exhibits a remarkable sequence homology among various counterparts in bacteria, plants, and mammals with more than half of the residues identical between bacterial and mammalian HSP60 (1-3). Whereas mammalian HSP60 is localized within the mitochondria, plant HSP60, or otherwise known as Rubisco-binding protein, is located in plant chloroplasts. It has been indicated that these proteins carry out a very important biological function due to the fact that HSP60 is present in so many different species. The common characteristics of the HSP60s from the divergent species are i) high abundance, ii) induction with environmental stress such as heat shock, iii) homo-oligomeric structures of either 7 or 14 subunits which reversibly dissociate in the presence of Mg2+ and ATP, iv) ATPase activity and v) a role in folding and assembly of oligomeric protein structures (4). These similarities are supported by recent studies where the single-ring human mitochondrial homolog, HSP60 with its co-chaperonin, HSP10 were expressed in a E. coli strain, engineered so that the groE operon is under strict regulatory control. This study has demonstrated that expression of HSP60-HSP10 was able to carry out all essential in vivo functions of GroEL and its co-chaperonin, GroES (5). Another important function of HSP60 and HSP10 is their protective functions against infection and cellular stress. HSP60 has however been linked to a number of autoimmune diseases, as well as Alzheimer's, coronary artery diseases, MS, and diabetes (6-9).
This product has been certified >90% pure using SDS-PAGE analysis. The protein has ATPase activity at the time of manufacture of 3.6µM phosphate liberated/hr/µg protein in a 200µl reaction at 37°C (pH7.5) in the presence of 20ul of 1mM ATP using a Malachite Green assay.
Cellular Localization:
Mitochondrion Matrix
References:
1. Hartl F.U. (1996) Nature. 381: 571-579. 2. Bukau B. and Horwich A.L. (1998) Cell. 92: 351-366. 3.Hartl F.U. and Hayer-Hartl M. (2002) Science. 295: 1852-1858. 4. Jindal S., et al. (1989) Molecular and Cellular Biol. 9: 2279-2283. 5. La Verda D., et al (1999) Infect Dis. Obstet. Gynecol. 7: 64-71. 6. Itoh H., et al. (2002) Eur. J. Biochem. 269: 5931-5938. 7.Gupta S. and Knowlton A.A. J. Cell Mol Med. 9: 51-58. 8. Deocaris C.C. et al. (2006) Cell Stress Chaperones. 11: 116-128. 9. Lai H.C., et al. (2007) Am. J. Physiol. Endocrinol. Metab. 292: E292-E297.
In both prokaryotic and eukaryotic cells, the misfolding and aggregation of proteins during biogenesis and under conditions of cellular stress are prevented by molecular chaperones. Members of the HSP60 family of heat shock proteins are some of the best characterized chaperones. HSP60, also known as Cpn60 or GroEl, is an abundant protein synthesized constitutively in the cell that is induced to a higher concentration after brief cell shock. It is present in many species and exhibits a remarkable sequence homology among various counterparts in bacteria, plants, and mammals with more than half of the residues identical between bacterial and mammalian HSP60 (1-3). Whereas mammalian HSP60 is localized within the mitochondria, plant HSP60, or otherwise known as Rubisco-binding protein, is located in plant chloroplasts. It has been indicated that these proteins carry out a very important biological function due to the fact that HSP60 is present in so many different species. The common characteristics of the HSP60s from the divergent species are i) high abundance, ii) induction with environmental stress such as heat shock, iii) homo-oligomeric structures of either 7 or 14 subunits which reversibly dissociate in the presence of Mg2+ and ATP, iv) ATPase activity and v) a role in folding and assembly of oligomeric protein structures (4). These similarities are supported by recent studies where the single-ring human mitochondrial homolog, HSP60 with its co-chaperonin, HSP10 were expressed in a E. coli strain, engineered so that the groE operon is under strict regulatory control. This study has demonstrated that expression of HSP60-HSP10 was able to carry out all essential in vivo functions of GroEL and its co-chaperonin, GroES (5). Another important function of HSP60 and HSP10 is their protective functions against infection and cellular stress. HSP60 has however been linked to a number of autoimmune diseases, as well as Alzheimer's, coronary artery diseases, MS, and diabetes (6-9).
This product has been certified >90% pure using SDS-PAGE analysis. The protein has ATPase activity at the time of manufacture of 3.6µM phosphate liberated/hr/µg protein in a 200µl reaction at 37°C (pH7.5) in the presence of 20ul of 1mM ATP using a Malachite Green assay.
Cellular Localization:
Mitochondrion Matrix
References:
1. Hartl F.U. (1996) Nature. 381: 571-579. 2. Bukau B. and Horwich A.L. (1998) Cell. 92: 351-366. 3.Hartl F.U. and Hayer-Hartl M. (2002) Science. 295: 1852-1858. 4. Jindal S., et al. (1989) Molecular and Cellular Biol. 9: 2279-2283. 5. La Verda D., et al (1999) Infect Dis. Obstet. Gynecol. 7: 64-71. 6. Itoh H., et al. (2002) Eur. J. Biochem. 269: 5931-5938. 7.Gupta S. and Knowlton A.A. J. Cell Mol Med. 9: 51-58. 8. Deocaris C.C. et al. (2006) Cell Stress Chaperones. 11: 116-128. 9. Lai H.C., et al. (2007) Am. J. Physiol. Endocrinol. Metab. 292: E292-E297.
HSP27s belong to an abundant and ubiquitous family of small heat shock proteins (sHSP). It is an important HSP found in both normal human cells and cancer cells. The basic structure of most sHSPs is a homologous and highly conserved amino acid sequence, with an ?-crystallin-domain at the C-terminus and the WD/EPF domain at the less conserved N-terminus. This N-terminus is essential for the development of high molecular oligomers (1, 2). HSP27-oligomers consist of stable dimers formed by as many as 8-40 HSP27 protein monomers (3). The oligomerization status is connected with the chaperone activity: aggregates of large oligomers have high chaperone activity, whereas dimers have no chaperone activity (4). HSP27 is localized to the cytoplasm of unstressed cells but can redistribute to the nucleus in response to stress, where it may function to stabilize DNA and/or the nuclear membrane. Other functions include chaperone activity (as mentioned above), thermo tolerance in vivo, inhibition of apoptosis, and signal transduction. Specifically, in vitro, it acts as an ATP-independent chaperone by inhibiting protein aggregation and by stabilizing partially denatured proteins, which ensures refolding of the HSP70 complex. HSP27 is also involved in the apoptotic signaling pathway because it interferes with the activation of cytochrome c/Apaf-1/dATP complex, thereby inhibiting the activation of procaspase-9. It is also hypothesized that HSP27 may serve some role in cross-bridge formation between actin and myosin (5). And finally, HSP27 is also thought to be involved in the process of cell differentiation. The up-regulation of HSP27 correlates with the rate of phosphorylation and with an increase of large oligomers. It is possible that HSP27 may play a crucial role in termination of growth (6). Looking for more information on HSP27? Visit our new HSP27 Scientific Resource Guide at http://www.HSP27.com.
This product has been certified >90% pure using SDS-PAGE analysis.
Cellular Localization:
Cytoplasm | Nucleus
References:
1. Kim K.K., Kim R., and Kim, S. (1998) Nature 394(6693): 595-599. 2. Van Montfort R., Slingsby C., and Vierling E. (2001) Addv Protein Chem. 59: 105-56. 3. Ehrnsperger M., Graber S., Gaestel M. and Buchner J. (1997) EMBO J. 16: 221-229. 4. Ciocca D.R., Oesterreich S., Chamness G.C., McGuire W.L., and Fugua S.A. (1993) J Natl Cancer Inst. 85 (19): 1558-70. 5. Sarto C. Binnz P.A. and Mocarelli P. (2000) Electrophoresis. 21(6): 1218-26. 6. Arrigo A.P. (2005) J Cell Biochem. 94(2): 241-6.
HSP27s belong to an abundant and ubiquitous family of small heat shock proteins (sHSP). It is an important HSP found in both normal human cells and cancer cells. The basic structure of most sHSPs is a homologous and highly conserved amino acid sequence, with an ?-crystallin-domain at the C-terminus and the WD/EPF domain at the less conserved N-terminus. This N-terminus is essential for the development of high molecular oligomers (1, 2). HSP27-oligomers consist of stable dimers formed by as many as 8-40 HSP27 protein monomers (3). The oligomerization status is connected with the chaperone activity: aggregates of large oligomers have high chaperone activity, whereas dimers have no chaperone activity (4). HSP27 is localized to the cytoplasm of unstressed cells but can redistribute to the nucleus in response to stress, where it may function to stabilize DNA and/or the nuclear membrane. Other functions include chaperone activity (as mentioned above), thermo tolerance in vivo, inhibition of apoptosis, and signal transduction. Specifically, in vitro, it acts as an ATP-independent chaperone by inhibiting protein aggregation and by stabilizing partially denatured proteins, which ensures refolding of the HSP70 complex. HSP27 is also involved in the apoptotic signaling pathway because it interferes with the activation of cytochrome c/Apaf-1/dATP complex, thereby inhibiting the activation of procaspase-9. It is also hypothesized that HSP27 may serve some role in cross-bridge formation between actin and myosin (5). And finally, HSP27 is also thought to be involved in the process of cell differentiation. The up-regulation of HSP27 correlates with the rate of phosphorylation and with an increase of large oligomers. It is possible that HSP27 may play a crucial role in termination of growth (6). Looking for more information on HSP27? Visit our new HSP27 Scientific Resource Guide at http://www.HSP27.com.
This product has been certified >90% pure using SDS-PAGE analysis.
Cellular Localization:
Cytoplasm | Nucleus
References:
1. Kim K.K., Kim R., and Kim, S. (1998) Nature 394(6693): 595-599. 2. Van Montfort R., Slingsby C., and Vierling E. (2001) Addv Protein Chem. 59: 105-56. 3. Ehrnsperger M., Graber S., Gaestel M. and Buchner J. (1997) EMBO J. 16: 221-229. 4. Ciocca D.R., Oesterreich S., Chamness G.C., McGuire W.L., and Fugua S.A. (1993) J Natl Cancer Inst. 85 (19): 1558-70. 5. Sarto C. Binnz P.A. and Mocarelli P. (2000) Electrophoresis. 21(6): 1218-26. 6. Arrigo A.P. (2005) J Cell Biochem. 94(2): 241-6.
HSP27s belong to an abundant and ubiquitous family of small heat shock proteins (sHSP). It is an important HSP found in both normal human cells and cancer cells. The basic structure of most sHSPs is a homologous and highly conserved amino acid sequence, with an ?-crystallin-domain at the C-terminus and the WD/EPF domain at the less conserved N-terminus. This N-terminus is essential for the development of high molecular oligomers (1, 2). HSP27-oligomers consist of stable dimers formed by as many as 8-40 HSP27 protein monomers (3). The oligomerization status is connected with the chaperone activity: aggregates of large oligomers have high chaperone activity, whereas dimers have no chaperone activity (4). HSP27 is localized to the cytoplasm of unstressed cells but can redistribute to the nucleus in response to stress, where it may function to stabilize DNA and/or the nuclear membrane. Other functions include chaperone activity (as mentioned above), thermo tolerance in vivo, inhibition of apoptosis, and signal transduction. Specifically, in vitro, it acts as an ATP-independent chaperone by inhibiting protein aggregation and by stabilizing partially denatured proteins, which ensures refolding of the HSP70 complex. HSP27 is also involved in the apoptotic signaling pathway because it interferes with the activation of cytochrome c/Apaf-1/dATP complex, thereby inhibiting the activation of procaspase-9. It is also hypothesized that HSP27 may serve some role in cross-bridge formation between actin and myosin (5). And finally, HSP27 is also thought to be involved in the process of cell differentiation. The up-regulation of HSP27 correlates with the rate of phosphorylation and with an increase of large oligomers. It is possible that HSP27 may play a crucial role in termination of growth (6). Looking for more information on HSP27? Visit our new HSP27 Scientific Resource Guide at http://www.HSP27.com.
This product has been certified >90% pure using SDS-PAGE analysis.
Cellular Localization:
Cytoplasm | Nucleus
References:
1. Kim K.K., Kim R., and Kim, S. (1998) Nature 394(6693): 595-599. 2. Van Montfort R., Slingsby C., and Vierling E. (2001) Addv Protein Chem. 59: 105-56. 3. Ehrnsperger M., Graber S., Gaestel M. and Buchner J. (1997) EMBO J. 16: 221-229. 4. Ciocca D.R., Oesterreich S., Chamness G.C., McGuire W.L., and Fugua S.A. (1993) J Natl Cancer Inst. 85 (19): 1558-70. 5. Sarto C. Binnz P.A. and Mocarelli P. (2000) Electrophoresis. 21(6): 1218-26. 6. Arrigo A.P. (2005) J Cell Biochem. 94(2): 241-6.
HSP70 genes encode abundant heat-inducible 70-kDa HSPs (HSP70s). In most eukaryotes HSP70 genes exist as part of a multigene family. They are found in most cellular compartments of eukaryotes including nuclei, mitochondria, chloroplasts, the endoplasmic reticulum and the cytosol, as well as in bacteria. The genes show a high degree of conservation, having at least 50% identity (2). The N-terminal two thirds of HSP70s are more conserved than the C-terminal third. HSP70 binds ATP with high affinity and possesses a weak ATPase activity which can be stimulated by binding to unfolded proteins and synthetic peptides (3). When HSC70 (constitutively expressed) present in mammalian cells was truncated, ATP binding activity was found to reside in an N-terminal fragment of 44 kDa which lacked peptide binding capacity. Polypeptide binding ability therefore resided within the C-terminal half (4). The structure of this ATP binding domain displays multiple features of nucleotide binding proteins (5). When cells are subjected to metabolic stress (e.g., heat shock) a member of the HSP 70 family, HSP 70 (HSP72), is expressed; HSP 70 is highly related to HSC70 (>90% sequence identity). Constitutively expressed HSC70 rapidly forms a stable complex with the highly inducible HSP70 in cells following heat shock. The interaction of HSC70 with HSP 70 is regulated by ATP. These two heat shock proteins move together in the cell experiencing stress. Furthermore, research on HSC70 has implicates it with a role in facilitating the recovery of centrosomal structure and function after heat shock (6).
This product has been certified >90% pure using SDS-PAGE analysis. The protein has ATPase activity at the time of manufacture of 3.2µM phosphate liberated/hr/µg protein in a 200µl reaction at 37°C (pH 8) in the presence of 20ul of 1mM ATP using a Malachite Green assay.
Cellular Localization:
Cytoplasm | Melanosome
References:
1. Brown C. L., et al. (1993) J.Cell Biol. 120(5): 1101-1112 2. Boorstein W. R., Ziegelhoffer T. & Craig E.A. (1993) J. Mol. Evol. 38(1): 1-17. 3. Rothman J. (1989) Cell. 59: 591 -601. 4. DeLuca-Flaherty et al. (1990) Cell. 62: 875-887. 5. Bork P., Sander C. & Valencia A. (1992) Proc. Natl Acad. Sci. USA. 89: 7290-7294. 6. Brown C. L., et al. (1996) J. Biol. Chem. 271(2): 833-840.
HSP70 genes encode abundant heat-inducible 70-kDa HSPs (HSP70s). In most eukaryotes HSP70 genes exist as part of a multigene family. They are found in most cellular compartments of eukaryotes including nuclei, mitochondria, chloroplasts, the endoplasmic reticulum and the cytosol, as well as in bacteria. The genes show a high degree of conservation, having at least 50% identity (2). The N-terminal two thirds of HSP70s are more conserved than the C-terminal third. HSP70 binds ATP with high affinity and possesses a weak ATPase activity which can be stimulated by binding to unfolded proteins and synthetic peptides (3). When HSC70 (constitutively expressed) present in mammalian cells was truncated, ATP binding activity was found to reside in an N-terminal fragment of 44 kDa which lacked peptide binding capacity. Polypeptide binding ability therefore resided within the C-terminal half (4). The structure of this ATP binding domain displays multiple features of nucleotide binding proteins (5). When cells are subjected to metabolic stress (e.g., heat shock) a member of the HSP 70 family, HSP 70 (HSP72), is expressed; HSP 70 is highly related to HSC70 (>90% sequence identity). Constitutively expressed HSC70 rapidly forms a stable complex with the highly inducible HSP70 in cells following heat shock. The interaction of HSC70 with HSP 70 is regulated by ATP. These two heat shock proteins move together in the cell experiencing stress. Furthermore, research on HSC70 has implicates it with a role in facilitating the recovery of centrosomal structure and function after heat shock (6).
This product has been certified >90% pure using SDS-PAGE analysis. The protein has ATPase activity at the time of manufacture of 3.2µM phosphate liberated/hr/µg protein in a 200µl reaction at 37°C (pH 8) in the presence of 20ul of 1mM ATP using a Malachite Green assay.
Cellular Localization:
Cytoplasm | Melanosome
References:
1. Brown C. L., et al. (1993) J.Cell Biol. 120(5): 1101-1112 2. Boorstein W. R., Ziegelhoffer T. & Craig E.A. (1993) J. Mol. Evol. 38(1): 1-17. 3. Rothman J. (1989) Cell. 59: 591 -601. 4. DeLuca-Flaherty et al. (1990) Cell. 62: 875-887. 5. Bork P., Sander C. & Valencia A. (1992) Proc. Natl Acad. Sci. USA. 89: 7290-7294. 6. Brown C. L., et al. (1996) J. Biol. Chem. 271(2): 833-840.
HSP70 genes encode abundant heat-inducible 70-kDa HSPs (HSP70s). In most eukaryotes HSP70 genes exist as part of a multigene family. They are found in most cellular compartments of eukaryotes including nuclei, mitochondria, chloroplasts, the endoplasmic reticulum and the cytosol, as well as in bacteria. The genes show a high degree of conservation, having at least 50% identity (2). The N-terminal two thirds of HSP70s are more conserved than the C-terminal third. HSP70 binds ATP with high affinity and possesses a weak ATPase activity which can be stimulated by binding to unfolded proteins and synthetic peptides (3). When HSC70 (constitutively expressed) present in mammalian cells was truncated, ATP binding activity was found to reside in an N-terminal fragment of 44 kDa which lacked peptide binding capacity. Polypeptide binding ability therefore resided within the C-terminal half (4). The structure of this ATP binding domain displays multiple features of nucleotide binding proteins (5). When cells are subjected to metabolic stress (e.g., heat shock) a member of the HSP 70 family, HSP 70 (HSP72), is expressed; HSP 70 is highly related to HSC70 (>90% sequence identity). Constitutively expressed HSC70 rapidly forms a stable complex with the highly inducible HSP70 in cells following heat shock. The interaction of HSC70 with HSP 70 is regulated by ATP. These two heat shock proteins move together in the cell experiencing stress. Furthermore, research on HSC70 has implicates it with a role in facilitating the recovery of centrosomal structure and function after heat shock (6).
This product has been certified >90% pure using SDS-PAGE analysis. The protein has ATPase activity at the time of manufacture of 3.2µM phosphate liberated/hr/µg protein in a 200µl reaction at 37°C (pH 8) in the presence of 20ul of 1mM ATP using a Malachite Green assay.
Cellular Localization:
Cytoplasm | Melanosome
References:
1. Brown C. L., et al. (1993) J.Cell Biol. 120(5): 1101-1112 2. Boorstein W. R., Ziegelhoffer T. & Craig E.A. (1993) J. Mol. Evol. 38(1): 1-17. 3. Rothman J. (1989) Cell. 59: 591 -601. 4. DeLuca-Flaherty et al. (1990) Cell. 62: 875-887. 5. Bork P., Sander C. & Valencia A. (1992) Proc. Natl Acad. Sci. USA. 89: 7290-7294. 6. Brown C. L., et al. (1996) J. Biol. Chem. 271(2): 833-840.
GRP78 is a ubiquitously expressed, 78-kDa glucose-regulated protein, and is commonly referred to as an immunoglobin chain binding protein (BiP). The BiP proteins are categorized as stress response proteins because they play an important role in the proper folding and assembly of nascent protein and in the scavenging of misfolded proteins in the endoplasmic reticulum lumen. Translation of BiP is directed by an internal ribosomal entry site (IRES) in the 5' non-translated region of the BiP mRNA. BiP IRES activity increases when cells are heat stressed (1). GRP78 is also critical for maintenance of cell homeostasis and the prevention of apoptosis (2). Luo et al. have provided findings that suggest GRP78 is essential for embryonic cell growth and pluripotent cell survival (3). In terms of diseases, GRP78 has been shown to be a reliable biomarker of hypoglycemia (Barnes), to serve a neuroprotective function in neurons exposed to glutamate and oxidative stress (4), and its protein levels are reduced in the brains of Alzheimer's patients (5). Also, the induction of the GRP78 protein that results in severe glucose and oxygen deprivation could possible lead to drug resistance to anti-tumor drugs (6, 7).
Cancer | Heat Shock | Cell Signaling | Protein Trafficking | Chaperone Proteins | Organelle Markers
Alternative Name(s):
BIP Protein, Grp78 Protein, HSPA5 Protein, MIF2 Protein, immunoglobulin heavy chain binding Protein
Category:
Recombinant
Accession Number:
NM_005347
Gene ID:
3309
Swiss-Prot:
P11021
Purification:
Affinity Purified
Concentration:
Lot/batch specific. See included datasheet.
Specificity:
~78 kDa
Certificate of Analysis:
This product has been certified >90% pure using SDS-PAGE analysis. The protein has ATPase activity at the time of manufacture of 2.3µM phosphate liberated/hr/µg protein in a 200µl reaction at 37°C (pH 8) in the presence of 20ul of 1mM ATP using a Malachite Green assay.
Cellular Localization:
Endoplasmic Reticulum Lumen | Melanosome
References:
1. Cho S., et al (2007) Mol Cell Biol. 27(1): 368-83. 2. Yang Y., et al. (1998) J Biol Chem. 273: 25552-25555. 3. Luo S., et al (2006) 26(15): 5688-97. 4. Yu Z., et al. (1999) Exp Neurol. 15: 302-314. 5. Koomagi R., et al. (1999) Anticancer Res. 19: 4333-4336. 6. Laquerre S., et al. (1998) J. Virology. 72: 4940-4949. 7. Dong D., et al. (2005) Cancer Res. 65(13): 5785-91.
GRP78 is a ubiquitously expressed, 78-kDa glucose-regulated protein, and is commonly referred to as an immunoglobin chain binding protein (BiP). The BiP proteins are categorized as stress response proteins because they play an important role in the proper folding and assembly of nascent protein and in the scavenging of misfolded proteins in the endoplasmic reticulum lumen. Translation of BiP is directed by an internal ribosomal entry site (IRES) in the 5' non-translated region of the BiP mRNA. BiP IRES activity increases when cells are heat stressed (1). GRP78 is also critical for maintenance of cell homeostasis and the prevention of apoptosis (2). Luo et al. have provided findings that suggest GRP78 is essential for embryonic cell growth and pluripotent cell survival (3). In terms of diseases, GRP78 has been shown to be a reliable biomarker of hypoglycemia (Barnes), to serve a neuroprotective function in neurons exposed to glutamate and oxidative stress (4), and its protein levels are reduced in the brains of Alzheimer's patients (5). Also, the induction of the GRP78 protein that results in severe glucose and oxygen deprivation could possible lead to drug resistance to anti-tumor drugs (6, 7).
Cancer | Heat Shock | Cell Signaling | Protein Trafficking | Chaperone Proteins | Organelle Markers
Alternative Name(s):
BIP Protein, Grp78 Protein, HSPA5 Protein, MIF2 Protein, immunoglobulin heavy chain binding Protein
Category:
Recombinant
Accession Number:
NM_005347
Gene ID:
3309
Swiss-Prot:
P11021
Purification:
Affinity Purified
Concentration:
Lot/batch specific. See included datasheet.
Specificity:
~78 kDa
Certificate of Analysis:
This product has been certified >90% pure using SDS-PAGE analysis. The protein has ATPase activity at the time of manufacture of 2.3µM phosphate liberated/hr/µg protein in a 200µl reaction at 37°C (pH 8) in the presence of 20ul of 1mM ATP using a Malachite Green assay.
Cellular Localization:
Endoplasmic Reticulum Lumen | Melanosome
References:
1. Cho S., et al (2007) Mol Cell Biol. 27(1): 368-83. 2. Yang Y., et al. (1998) J Biol Chem. 273: 25552-25555. 3. Luo S., et al (2006) 26(15): 5688-97. 4. Yu Z., et al. (1999) Exp Neurol. 15: 302-314. 5. Koomagi R., et al. (1999) Anticancer Res. 19: 4333-4336. 6. Laquerre S., et al. (1998) J. Virology. 72: 4940-4949. 7. Dong D., et al. (2005) Cancer Res. 65(13): 5785-91.
GRP78 is a ubiquitously expressed, 78-kDa glucose-regulated protein, and is commonly referred to as an immunoglobin chain binding protein (BiP). The BiP proteins are categorized as stress response proteins because they play an important role in the proper folding and assembly of nascent protein and in the scavenging of misfolded proteins in the endoplasmic reticulum lumen. Translation of BiP is directed by an internal ribosomal entry site (IRES) in the 5' non-translated region of the BiP mRNA. BiP IRES activity increases when cells are heat stressed (1). GRP78 is also critical for maintenance of cell homeostasis and the prevention of apoptosis (2). Luo et al. have provided findings that suggest GRP78 is essential for embryonic cell growth and pluripotent cell survival (3). In terms of diseases, GRP78 has been shown to be a reliable biomarker of hypoglycemia (Barnes), to serve a neuroprotective function in neurons exposed to glutamate and oxidative stress (4), and its protein levels are reduced in the brains of Alzheimer's patients (5). Also, the induction of the GRP78 protein that results in severe glucose and oxygen deprivation could possible lead to drug resistance to anti-tumor drugs (6, 7).
Cancer | Heat Shock | Cell Signaling | Protein Trafficking | Chaperone Proteins | Organelle Markers
Alternative Name(s):
BIP Protein, Grp78 Protein, HSPA5 Protein, MIF2 Protein, immunoglobulin heavy chain binding Protein
Category:
Recombinant
Accession Number:
NM_005347
Gene ID:
3309
Swiss-Prot:
P11021
Purification:
Affinity Purified
Concentration:
Lot/batch specific. See included datasheet.
Specificity:
~78 kDa
Certificate of Analysis:
This product has been certified >90% pure using SDS-PAGE analysis. The protein has ATPase activity at the time of manufacture of 2.3µM phosphate liberated/hr/µg protein in a 200µl reaction at 37°C (pH 8) in the presence of 20ul of 1mM ATP using a Malachite Green assay.
Cellular Localization:
Endoplasmic Reticulum Lumen | Melanosome
References:
1. Cho S., et al (2007) Mol Cell Biol. 27(1): 368-83. 2. Yang Y., et al. (1998) J Biol Chem. 273: 25552-25555. 3. Luo S., et al (2006) 26(15): 5688-97. 4. Yu Z., et al. (1999) Exp Neurol. 15: 302-314. 5. Koomagi R., et al. (1999) Anticancer Res. 19: 4333-4336. 6. Laquerre S., et al. (1998) J. Virology. 72: 4940-4949. 7. Dong D., et al. (2005) Cancer Res. 65(13): 5785-91.
Active Human Recombinant HSP70 Full Length Protein
Background Info:
HSP70 genes encode abundant heat-inducible 70-kDa HSPs (HSP70s). In most eukaryotes HSP70 genes exist as part of a multigene family. They are found in most cellular compartments of eukaryotes including nuclei, mitochondria, chloroplasts, the endoplasmic reticulum and the cytosol, as well as in bacteria. The genes show a high degree of conservation, having at least 50% identity (2). The N-terminal two thirds of HSP70s are more conserved than the C-terminal third. HSP70 binds ATP with high affinity and possesses a weak ATPase activity which can be stimulated by binding to unfolded proteins and synthetic peptides (3). When HSC70 (constitutively expressed) present in mammalian cells was truncated, ATP binding activity was found to reside in an N-terminal fragment of 44kDa which lacked peptide binding capacity. Polypeptide binding ability therefore resided within the C-terminal half (4). The structure of this ATP binding domain displays multiple features of nucleotide binding proteins (5). All HSP70s, regardless of location, bind proteins, particularly unfolded ones. The molecular chaperones of the HSP70 family recognize and bind to nascent polypeptide chains as well as partially folded intermediates of proteins preventing their aggregation and misfolding. The binding of ATP triggers a critical conformational change leading to the release of the bound substrate protein (6). The universal ability of HSP70s to undergo cycles of binding to and release from hydrophobic stretches of partially unfolded proteins determines their role in a great variety of vital intracellular functions such as protein synthesis, protein folding and oligomerization and protein transport. Looking for more information on HSP70? Visit our new HSP70 Scientific Resource Guide at http://www.HSP70.com.
This product has been certified >95% pure using SDS-PAGE analysis. The protein has ATPase activity at the time of manufacture of 3.0µM phosphate liberated/hr/µg protein in a 200µl reaction at 37°C (pH7.5) in the presence of 20ul of 1mM ATP using a Malachite Green assay.
Cellular Localization:
Cytoplasm
References:
1. Zho J. (1998) Cell. 94: 471-480. 2. Boorstein, W. R., Ziegelhoffer, T. & Craig, E. A. (1993) J. Mol. Evol. 38(1): 1-17. 3. Rothman J. (1989) Cell. 59: 591 -601. 4. DeLuca-Flaherty et al. (1990) Cell. 62: 875-887. 5. Bork P., Sander C. & Valencia A. (1992) Proc. Natl Acad. Sci. USA. 89: 7290-7294. 6. Fink A.L. (1999) Physiol. Rev. 79: 425-449. 7. Smith D.F., et al., (1993) Mol. Cell. Biol. 13(2): 869-876. 8. Prapapanich V., et al., (1996) Mol. Cell. Biol. 16(11): 6200-6207. 9. Fernandez-Funez et al., (2000) Nature. 408(6808): 101-106.
Active Human Recombinant HSP70 Full Length Protein
Background Info:
HSP70 genes encode abundant heat-inducible 70-kDa HSPs (HSP70s). In most eukaryotes HSP70 genes exist as part of a multigene family. They are found in most cellular compartments of eukaryotes including nuclei, mitochondria, chloroplasts, the endoplasmic reticulum and the cytosol, as well as in bacteria. The genes show a high degree of conservation, having at least 50% identity (2). The N-terminal two thirds of HSP70s are more conserved than the C-terminal third. HSP70 binds ATP with high affinity and possesses a weak ATPase activity which can be stimulated by binding to unfolded proteins and synthetic peptides (3). When HSC70 (constitutively expressed) present in mammalian cells was truncated, ATP binding activity was found to reside in an N-terminal fragment of 44kDa which lacked peptide binding capacity. Polypeptide binding ability therefore resided within the C-terminal half (4). The structure of this ATP binding domain displays multiple features of nucleotide binding proteins (5). All HSP70s, regardless of location, bind proteins, particularly unfolded ones. The molecular chaperones of the HSP70 family recognize and bind to nascent polypeptide chains as well as partially folded intermediates of proteins preventing their aggregation and misfolding. The binding of ATP triggers a critical conformational change leading to the release of the bound substrate protein (6). The universal ability of HSP70s to undergo cycles of binding to and release from hydrophobic stretches of partially unfolded proteins determines their role in a great variety of vital intracellular functions such as protein synthesis, protein folding and oligomerization and protein transport. Looking for more information on HSP70? Visit our new HSP70 Scientific Resource Guide at http://www.HSP70.com.
This product has been certified >95% pure using SDS-PAGE analysis. The protein has ATPase activity at the time of manufacture of 3.0µM phosphate liberated/hr/µg protein in a 200µl reaction at 37°C (pH7.5) in the presence of 20ul of 1mM ATP using a Malachite Green assay.
Cellular Localization:
Cytoplasm
References:
1. Zho J. (1998) Cell. 94: 471-480. 2. Boorstein, W. R., Ziegelhoffer, T. & Craig, E. A. (1993) J. Mol. Evol. 38(1): 1-17. 3. Rothman J. (1989) Cell. 59: 591 -601. 4. DeLuca-Flaherty et al. (1990) Cell. 62: 875-887. 5. Bork P., Sander C. & Valencia A. (1992) Proc. Natl Acad. Sci. USA. 89: 7290-7294. 6. Fink A.L. (1999) Physiol. Rev. 79: 425-449. 7. Smith D.F., et al., (1993) Mol. Cell. Biol. 13(2): 869-876. 8. Prapapanich V., et al., (1996) Mol. Cell. Biol. 16(11): 6200-6207. 9. Fernandez-Funez et al., (2000) Nature. 408(6808): 101-106.
Active Human Recombinant HSP70 Full Length Protein
Background Info:
HSP70 genes encode abundant heat-inducible 70-kDa HSPs (HSP70s). In most eukaryotes HSP70 genes exist as part of a multigene family. They are found in most cellular compartments of eukaryotes including nuclei, mitochondria, chloroplasts, the endoplasmic reticulum and the cytosol, as well as in bacteria. The genes show a high degree of conservation, having at least 50% identity (2). The N-terminal two thirds of HSP70s are more conserved than the C-terminal third. HSP70 binds ATP with high affinity and possesses a weak ATPase activity which can be stimulated by binding to unfolded proteins and synthetic peptides (3). When HSC70 (constitutively expressed) present in mammalian cells was truncated, ATP binding activity was found to reside in an N-terminal fragment of 44kDa which lacked peptide binding capacity. Polypeptide binding ability therefore resided within the C-terminal half (4). The structure of this ATP binding domain displays multiple features of nucleotide binding proteins (5). All HSP70s, regardless of location, bind proteins, particularly unfolded ones. The molecular chaperones of the HSP70 family recognize and bind to nascent polypeptide chains as well as partially folded intermediates of proteins preventing their aggregation and misfolding. The binding of ATP triggers a critical conformational change leading to the release of the bound substrate protein (6). The universal ability of HSP70s to undergo cycles of binding to and release from hydrophobic stretches of partially unfolded proteins determines their role in a great variety of vital intracellular functions such as protein synthesis, protein folding and oligomerization and protein transport. Looking for more information on HSP70? Visit our new HSP70 Scientific Resource Guide at http://www.HSP70.com.
This product has been certified >95% pure using SDS-PAGE analysis. The protein has ATPase activity at the time of manufacture of 3.0µM phosphate liberated/hr/µg protein in a 200µl reaction at 37°C (pH7.5) in the presence of 20ul of 1mM ATP using a Malachite Green assay.
Cellular Localization:
Cytoplasm
References:
1. Zho J. (1998) Cell. 94: 471-480. 2. Boorstein, W. R., Ziegelhoffer, T. & Craig, E. A. (1993) J. Mol. Evol. 38(1): 1-17. 3. Rothman J. (1989) Cell. 59: 591 -601. 4. DeLuca-Flaherty et al. (1990) Cell. 62: 875-887. 5. Bork P., Sander C. & Valencia A. (1992) Proc. Natl Acad. Sci. USA. 89: 7290-7294. 6. Fink A.L. (1999) Physiol. Rev. 79: 425-449. 7. Smith D.F., et al., (1993) Mol. Cell. Biol. 13(2): 869-876. 8. Prapapanich V., et al., (1996) Mol. Cell. Biol. 16(11): 6200-6207. 9. Fernandez-Funez et al., (2000) Nature. 408(6808): 101-106.
HSP70 genes encode abundant heat-inducible 70-kDa HSPs (HSP70s). In most eukaryotes HSP70 genes exist as part of a multigene family. They are found in most cellular compartments of eukaryotes including nuclei, mitochondria, chloroplasts, the endoplasmic reticulum and the cytosol, as well as in bacteria. The genes show a high degree of conservation, having at least 50% identity (2). The N-terminal two thirds of HSP70s are more conserved than the C-terminal third. HSP70 binds ATP with high affinity and possesses a weak ATPase activity which can be stimulated by binding to unfolded proteins and synthetic peptides (3). When HSC70 (constitutively expressed) present in mammalian cells was truncated, ATP binding activity was found to reside in an N-terminal fragment of 44kDa which lacked peptide binding capacity. Polypeptide binding ability therefore resided within the C-terminal half (4). The structure of this ATP binding domain displays multiple features of nucleotide binding proteins (5). All HSP70s, regardless of location, bind proteins, particularly unfolded ones. The molecular chaperones of the HSP70 family recognize and bind to nascent polypeptide chains as well as partially folded intermediates of proteins preventing their aggregation and misfolding. The binding of ATP triggers a critical conformational change leading to the release of the bound substrate protein (6). The universal ability of HSP70s to undergo cycles of binding to and release from hydrophobic stretches of partially unfolded proteins determines their role in a great variety of vital intracellular functions such as protein synthesis, protein folding and oligomerization and protein transport. Looking for more information on HSP70? Visit our new HSP70 Scientific Resource Guide at http://www.HSP70.com.
HSP70 genes encode abundant heat-inducible 70-kDa HSPs (HSP70s). In most eukaryotes HSP70 genes exist as part of a multigene family. They are found in most cellular compartments of eukaryotes including nuclei, mitochondria, chloroplasts, the endoplasmic reticulum and the cytosol, as well as in bacteria. The genes show a high degree of conservation, having at least 50% identity (2). The N-terminal two thirds of HSP70s are more conserved than the C-terminal third. HSP70 binds ATP with high affinity and possesses a weak ATPase activity which can be stimulated by binding to unfolded proteins and synthetic peptides (3). When HSC70 (constitutively expressed) present in mammalian cells was truncated, ATP binding activity was found to reside in an N-terminal fragment of 44kDa which lacked peptide binding capacity. Polypeptide binding ability therefore resided within the C-terminal half (4). The structure of this ATP binding domain displays multiple features of nucleotide binding proteins (5). All HSP70s, regardless of location, bind proteins, particularly unfolded ones. The molecular chaperones of the HSP70 family recognize and bind to nascent polypeptide chains as well as partially folded intermediates of proteins preventing their aggregation and misfolding. The binding of ATP triggers a critical conformational change leading to the release of the bound substrate protein (6). The universal ability of HSP70s to undergo cycles of binding to and release from hydrophobic stretches of partially unfolded proteins determines their role in a great variety of vital intracellular functions such as protein synthesis, protein folding and oligomerization and protein transport. Looking for more information on HSP70? Visit our new HSP70 Scientific Resource Guide at http://www.HSP70.com.
HSP70 genes encode abundant heat-inducible 70-kDa HSPs (HSP70s). In most eukaryotes HSP70 genes exist as part of a multigene family. They are found in most cellular compartments of eukaryotes including nuclei, mitochondria, chloroplasts, the endoplasmic reticulum and the cytosol, as well as in bacteria. The genes show a high degree of conservation, having at least 50% identity (2). The N-terminal two thirds of HSP70s are more conserved than the C-terminal third. HSP70 binds ATP with high affinity and possesses a weak ATPase activity which can be stimulated by binding to unfolded proteins and synthetic peptides (3). When HSC70 (constitutively expressed) present in mammalian cells was truncated, ATP binding activity was found to reside in an N-terminal fragment of 44kDa which lacked peptide binding capacity. Polypeptide binding ability therefore resided within the C-terminal half (4). The structure of this ATP binding domain displays multiple features of nucleotide binding proteins (5). All HSP70s, regardless of location, bind proteins, particularly unfolded ones. The molecular chaperones of the HSP70 family recognize and bind to nascent polypeptide chains as well as partially folded intermediates of proteins preventing their aggregation and misfolding. The binding of ATP triggers a critical conformational change leading to the release of the bound substrate protein (6). The universal ability of HSP70s to undergo cycles of binding to and release from hydrophobic stretches of partially unfolded proteins determines their role in a great variety of vital intracellular functions such as protein synthesis, protein folding and oligomerization and protein transport. Looking for more information on HSP70? Visit our new HSP70 Scientific Resource Guide at http://www.HSP70.com.
Mycobacterium bovis BCG Recombinant HSP65 Partial Protein
Background Info:
HSP65 isolated from Mycobacterium bovis BCG, is a member of the HSP60 family of heat shock proteins (2, 3). HSP60s are mitochondrial chaperonins that are typically held responsible for the transportation and refolding of proteins from the cytoplasm into the mitochondrial matrix. In addition to its role as a heat shock protein, HSP60 functions as a chaperonin to assist in folding linear amino acid chains into their respective three-dimensional structure. HSP60s are a ubiquitous class of HSPs that specifically promote the folding and assembly of cellular polypeptides in an ATP-dependent manner (1). Specifically, sequence comparison of HSP65 from different mycobacterium strains showed that the protein sequence of M. bovis BCG is identical to that of M. tuberculosis, and very similar to that of M. leprae, the pathogens that cause tuberculosis and tuberculoid leprosy, respectively (2,4). Mycobacterium bovis BCG HSP65 was identified as the immunodominant antigen during mycobacterial diseases and vaccination. It is also believed to be the antigen that induces autoimmune disease, such as adjuvant arthritis in rats (5, 6).
Product Type:
Protein
Format:
20mM Tris, 150mM NaCl, 10% glycerol
Storage Temp:
-20ºC
Applications:
WB | SDS-PAGE | Functional Assay | ELISA
Target:
HSP65
Conjugate:
No tag
Research Area(s):
Cancer | Heat Shock
Alternative Name(s):
60kDa chaperonin 2 Protein, Antigen A Protein, Cell wall protein A Protein, groEL Protein, GroEL2 Protein, GroL2 Protein, M. Tuberculosis cell wall protein A Protein, M. Tuberculosis HSP65 Protein, Protein Cpm60 2 Protein
Category:
Recombinant
Accession Number:
AAQ64501.1
Swiss-Prot:
Q1EHB9
Purification:
Multi-Step Purified
Concentration:
Lot/batch specific. See included datasheet.
Specificity:
~65 kDa
Certificate of Analysis:
This product has been certified >90% pure using SDS-PAGE analysis.
Cellular Localization:
Cytoplasm
References:
1. Koll H., et al. (1992) Cell. 68: 1163-1175. 2. Thole J.E.R., et al. (1985) Infect. Immuno. 50: 800-806. 3. Thole J.E.R., et al., (1987) Infect. Immuno. 55: 1466-1475. 4. Shinnick T.M. Sweetser D., Thole J., van Embden J. and Young R.A. (1987) Infect. Immuno. 55: 1932-1935. 5. Van Eden W., et al. (1988) Nature 331: 171-178. 6. Cobelens P.M., et al. (2002) Rheumatology 41: 775-779.
Mycobacterium bovis BCG Recombinant HSP65 Partial Protein
Background Info:
HSP65 isolated from Mycobacterium bovis BCG, is a member of the HSP60 family of heat shock proteins (2, 3). HSP60s are mitochondrial chaperonins that are typically held responsible for the transportation and refolding of proteins from the cytoplasm into the mitochondrial matrix. In addition to its role as a heat shock protein, HSP60 functions as a chaperonin to assist in folding linear amino acid chains into their respective three-dimensional structure. HSP60s are a ubiquitous class of HSPs that specifically promote the folding and assembly of cellular polypeptides in an ATP-dependent manner (1). Specifically, sequence comparison of HSP65 from different mycobacterium strains showed that the protein sequence of M. bovis BCG is identical to that of M. tuberculosis, and very similar to that of M. leprae, the pathogens that cause tuberculosis and tuberculoid leprosy, respectively (2,4). Mycobacterium bovis BCG HSP65 was identified as the immunodominant antigen during mycobacterial diseases and vaccination. It is also believed to be the antigen that induces autoimmune disease, such as adjuvant arthritis in rats (5, 6).
Product Type:
Protein
Format:
20mM Tris, 150mM NaCl, 10% glycerol
Storage Temp:
-20ºC
Applications:
WB | SDS-PAGE | Functional Assay | ELISA
Target:
HSP65
Conjugate:
No tag
Research Area(s):
Cancer | Heat Shock
Alternative Name(s):
60kDa chaperonin 2 Protein, Antigen A Protein, Cell wall protein A Protein, groEL Protein, GroEL2 Protein, GroL2 Protein, M. Tuberculosis cell wall protein A Protein, M. Tuberculosis HSP65 Protein, Protein Cpm60 2 Protein
Category:
Recombinant
Accession Number:
AAQ64501.1
Swiss-Prot:
Q1EHB9
Purification:
Multi-Step Purified
Concentration:
Lot/batch specific. See included datasheet.
Specificity:
~65 kDa
Certificate of Analysis:
This product has been certified >90% pure using SDS-PAGE analysis.
Cellular Localization:
Cytoplasm
References:
1. Koll H., et al. (1992) Cell. 68: 1163-1175. 2. Thole J.E.R., et al. (1985) Infect. Immuno. 50: 800-806. 3. Thole J.E.R., et al., (1987) Infect. Immuno. 55: 1466-1475. 4. Shinnick T.M. Sweetser D., Thole J., van Embden J. and Young R.A. (1987) Infect. Immuno. 55: 1932-1935. 5. Van Eden W., et al. (1988) Nature 331: 171-178. 6. Cobelens P.M., et al. (2002) Rheumatology 41: 775-779.
Mycobacterium bovis BCG Recombinant HSP65 Partial Protein
Background Info:
HSP65 isolated from Mycobacterium bovis BCG, is a member of the HSP60 family of heat shock proteins (2, 3). HSP60s are mitochondrial chaperonins that are typically held responsible for the transportation and refolding of proteins from the cytoplasm into the mitochondrial matrix. In addition to its role as a heat shock protein, HSP60 functions as a chaperonin to assist in folding linear amino acid chains into their respective three-dimensional structure. HSP60s are a ubiquitous class of HSPs that specifically promote the folding and assembly of cellular polypeptides in an ATP-dependent manner (1). Specifically, sequence comparison of HSP65 from different mycobacterium strains showed that the protein sequence of M. bovis BCG is identical to that of M. tuberculosis, and very similar to that of M. leprae, the pathogens that cause tuberculosis and tuberculoid leprosy, respectively (2,4). Mycobacterium bovis BCG HSP65 was identified as the immunodominant antigen during mycobacterial diseases and vaccination. It is also believed to be the antigen that induces autoimmune disease, such as adjuvant arthritis in rats (5, 6).
Product Type:
Protein
Format:
20mM Tris, 150mM NaCl, 10% glycerol
Storage Temp:
-20ºC
Applications:
WB | SDS-PAGE | Functional Assay | ELISA
Target:
HSP65
Conjugate:
No tag
Research Area(s):
Cancer | Heat Shock
Alternative Name(s):
60kDa chaperonin 2 Protein, Antigen A Protein, Cell wall protein A Protein, groEL Protein, GroEL2 Protein, GroL2 Protein, M. Tuberculosis cell wall protein A Protein, M. Tuberculosis HSP65 Protein, Protein Cpm60 2 Protein
Category:
Recombinant
Accession Number:
AAQ64501.1
Swiss-Prot:
Q1EHB9
Purification:
Multi-Step Purified
Concentration:
Lot/batch specific. See included datasheet.
Specificity:
~65 kDa
Certificate of Analysis:
This product has been certified >90% pure using SDS-PAGE analysis.
Cellular Localization:
Cytoplasm
References:
1. Koll H., et al. (1992) Cell. 68: 1163-1175. 2. Thole J.E.R., et al. (1985) Infect. Immuno. 50: 800-806. 3. Thole J.E.R., et al., (1987) Infect. Immuno. 55: 1466-1475. 4. Shinnick T.M. Sweetser D., Thole J., van Embden J. and Young R.A. (1987) Infect. Immuno. 55: 1932-1935. 5. Van Eden W., et al. (1988) Nature 331: 171-178. 6. Cobelens P.M., et al. (2002) Rheumatology 41: 775-779.
HSP70 genes encode abundant heat-inducible 70-kDa HSPs (HSP70s). In most eukaryotes HSP70 genes exist as part of a multigene family. They are found in most cellular compartments of eukaryotes including nuclei, mitochondria, chloroplasts, the endoplasmic reticulum and the cytosol, as well as in bacteria. The genes show a high degree of conservation, having at least 50% identity (2). The N-terminal two thirds of HSP70s are more conserved than the C-terminal third. HSP70 binds ATP with high affinity and possesses a weak ATPase activity which can be stimulated by binding to unfolded proteins and synthetic peptides (3). When HSC70 (constitutively expressed) present in mammalian cells was truncated, ATP binding activity was found to reside in an N-terminal fragment of 44kDa which lacked peptide binding capacity. Polypeptide binding ability therefore resided within the C-terminal half (4). The structure of this ATP binding domain displays multiple features of nucleotide binding proteins (5). All HSP70s, regardless of location, bind proteins, particularly unfolded ones. The molecular chaperones of the HSP70 family recognize and bind to nascent polypeptide chains as well as partially folded intermediates of proteins preventing their aggregation and misfolding. The binding of ATP triggers a critical conformational change leading to the release of the bound substrate protein (6). The universal ability of HSP70s to undergo cycles of binding to and release from hydrophobic stretches of partially unfolded proteins determines their role in a great variety of vital intracellular functions such as protein synthesis, protein folding and oligomerization and protein transport. Looking for more information on HSP70? Visit our new HSP70 Scientific Resource Guide at http://www.HSP70.com.
This product has been certified >90% pure using SDS-PAGE analysis. The protein tested positive for ATPase activity using a Malachite Green assay.
Cellular Localization:
Cytoplasm
References:
1. Zho J. (1998) Cell. 94: 471-480. 2. Boorstein W. R., Ziegelhoffer T. & Craig E. A. (1993) J. Mol. Evol.38(1): 1-17. 3. Rothman J. (1989) Cell. 59: 591 -601. 4. DeLuca-Flaherty et al. (1990) Cell. 62: 875-887. 5. Bork P., Sander C. & Valencia A. (1992) Proc. Natl Acad. Sci. USA. 89: 7290-7294. 6. Fink A.L. (1999) Physiol. Rev. 79: 425-449.
HSP70 genes encode abundant heat-inducible 70-kDa HSPs (HSP70s). In most eukaryotes HSP70 genes exist as part of a multigene family. They are found in most cellular compartments of eukaryotes including nuclei, mitochondria, chloroplasts, the endoplasmic reticulum and the cytosol, as well as in bacteria. The genes show a high degree of conservation, having at least 50% identity (2). The N-terminal two thirds of HSP70s are more conserved than the C-terminal third. HSP70 binds ATP with high affinity and possesses a weak ATPase activity which can be stimulated by binding to unfolded proteins and synthetic peptides (3). When HSC70 (constitutively expressed) present in mammalian cells was truncated, ATP binding activity was found to reside in an N-terminal fragment of 44kDa which lacked peptide binding capacity. Polypeptide binding ability therefore resided within the C-terminal half (4). The structure of this ATP binding domain displays multiple features of nucleotide binding proteins (5). All HSP70s, regardless of location, bind proteins, particularly unfolded ones. The molecular chaperones of the HSP70 family recognize and bind to nascent polypeptide chains as well as partially folded intermediates of proteins preventing their aggregation and misfolding. The binding of ATP triggers a critical conformational change leading to the release of the bound substrate protein (6). The universal ability of HSP70s to undergo cycles of binding to and release from hydrophobic stretches of partially unfolded proteins determines their role in a great variety of vital intracellular functions such as protein synthesis, protein folding and oligomerization and protein transport. Looking for more information on HSP70? Visit our new HSP70 Scientific Resource Guide at http://www.HSP70.com.
This product has been certified >90% pure using SDS-PAGE analysis. The protein tested positive for ATPase activity using a Malachite Green assay.
Cellular Localization:
Cytoplasm
References:
1. Zho J. (1998) Cell. 94: 471-480. 2. Boorstein W. R., Ziegelhoffer T. & Craig E. A. (1993) J. Mol. Evol.38(1): 1-17. 3. Rothman J. (1989) Cell. 59: 591 -601. 4. DeLuca-Flaherty et al. (1990) Cell. 62: 875-887. 5. Bork P., Sander C. & Valencia A. (1992) Proc. Natl Acad. Sci. USA. 89: 7290-7294. 6. Fink A.L. (1999) Physiol. Rev. 79: 425-449.
HSP70 genes encode abundant heat-inducible 70-kDa HSPs (HSP70s). In most eukaryotes HSP70 genes exist as part of a multigene family. They are found in most cellular compartments of eukaryotes including nuclei, mitochondria, chloroplasts, the endoplasmic reticulum and the cytosol, as well as in bacteria. The genes show a high degree of conservation, having at least 50% identity (2). The N-terminal two thirds of HSP70s are more conserved than the C-terminal third. HSP70 binds ATP with high affinity and possesses a weak ATPase activity which can be stimulated by binding to unfolded proteins and synthetic peptides (3). When HSC70 (constitutively expressed) present in mammalian cells was truncated, ATP binding activity was found to reside in an N-terminal fragment of 44kDa which lacked peptide binding capacity. Polypeptide binding ability therefore resided within the C-terminal half (4). The structure of this ATP binding domain displays multiple features of nucleotide binding proteins (5). All HSP70s, regardless of location, bind proteins, particularly unfolded ones. The molecular chaperones of the HSP70 family recognize and bind to nascent polypeptide chains as well as partially folded intermediates of proteins preventing their aggregation and misfolding. The binding of ATP triggers a critical conformational change leading to the release of the bound substrate protein (6). The universal ability of HSP70s to undergo cycles of binding to and release from hydrophobic stretches of partially unfolded proteins determines their role in a great variety of vital intracellular functions such as protein synthesis, protein folding and oligomerization and protein transport. Looking for more information on HSP70? Visit our new HSP70 Scientific Resource Guide at http://www.HSP70.com.
This product has been certified >90% pure using SDS-PAGE analysis. The protein tested positive for ATPase activity using a Malachite Green assay.
Cellular Localization:
Cytoplasm
References:
1. Zho J. (1998) Cell. 94: 471-480. 2. Boorstein W. R., Ziegelhoffer T. & Craig E. A. (1993) J. Mol. Evol.38(1): 1-17. 3. Rothman J. (1989) Cell. 59: 591 -601. 4. DeLuca-Flaherty et al. (1990) Cell. 62: 875-887. 5. Bork P., Sander C. & Valencia A. (1992) Proc. Natl Acad. Sci. USA. 89: 7290-7294. 6. Fink A.L. (1999) Physiol. Rev. 79: 425-449.
HSP27s belong to an abundant and ubiquitous family of small heat shock proteins (sHSP). It is an important HSP found in both normal human cells and cancer cells. The basic structure of most sHSPs is a homologous and highly conserved amino acid sequence, with an ?-crystallin-domain at the C-terminus and the WD/EPF domain at the less conserved N-terminus. This N-terminus is essential for the development of high molecular oligomers (1, 2). HSP27-oligomers consist of stable dimers formed by as many as 8-40 HSP27 protein monomers (3). The oligomerization status is connected with the chaperone activity: aggregates of large oligomers have high chaperone activity, whereas dimers have no chaperone activity (4). HSP27 is localized to the cytoplasm of unstressed cells but can redistribute to the nucleus in response to stress, where it may function to stabilize DNA and/or the nuclear membrane. Other functions include chaperone activity (as mentioned above), thermo tolerance in vivo, inhibition of apoptosis, and signal transduction. Specifically, in vitro, it acts as an ATP-independent chaperone by inhibiting protein aggregation and by stabilizing partially denatured proteins, which ensures refolding of the HSP70 complex. HSP27 is also involved in the apoptotic signaling pathway because it interferes with the activation of cytochrome c/Apaf-1/dATP complex, thereby inhibiting the activation of procaspase-9. It is also hypothesized that HSP27 may serve some role in cross-bridge formation between actin and myosin (5). And finally, HSP27 is also thought to be involved in the process of cell differentiation. The up-regulation of HSP27 correlates with the rate of phosphorylation and with an increase of large oligomers. It is possible that HSP27 may play a crucial role in termination of growth (6). Looking for more information on HSP27? Visit our new HSP27 Scientific Resource Guide at http://www.HSP27.com.
This product has been certified >90% pure using SDS-PAGE analysis.
Cellular Localization:
Cytoplasm | Nucleus
References:
1. Kim K.K., Kim R., and Kim, S. (1998) Nature 394(6693): 595-599. 2. Van Montfort R., Slingsby C., and Vierling E. (2001) Addv Protein Chem. 59: 105-56. 3. Ehrnsperger M., Graber S., Gaestel M. and Buchner J. (1997) EMBO J. 16: 221-229. 4. Ciocca D.R., Oesterreich S., Chamness G.C., McGuire W.L., and Fugua S.A. (1993) J Natl Cancer Inst. 85 (19): 1558-70. 5. Sarto C. Binnz P.A. and Mocarelli P. (2000) Electrophoresis. 21(6): 1218-26. 6. Arrigo A.P. (2005) J Cell Biochem. 94(2): 241-6.
HSP27s belong to an abundant and ubiquitous family of small heat shock proteins (sHSP). It is an important HSP found in both normal human cells and cancer cells. The basic structure of most sHSPs is a homologous and highly conserved amino acid sequence, with an ?-crystallin-domain at the C-terminus and the WD/EPF domain at the less conserved N-terminus. This N-terminus is essential for the development of high molecular oligomers (1, 2). HSP27-oligomers consist of stable dimers formed by as many as 8-40 HSP27 protein monomers (3). The oligomerization status is connected with the chaperone activity: aggregates of large oligomers have high chaperone activity, whereas dimers have no chaperone activity (4). HSP27 is localized to the cytoplasm of unstressed cells but can redistribute to the nucleus in response to stress, where it may function to stabilize DNA and/or the nuclear membrane. Other functions include chaperone activity (as mentioned above), thermo tolerance in vivo, inhibition of apoptosis, and signal transduction. Specifically, in vitro, it acts as an ATP-independent chaperone by inhibiting protein aggregation and by stabilizing partially denatured proteins, which ensures refolding of the HSP70 complex. HSP27 is also involved in the apoptotic signaling pathway because it interferes with the activation of cytochrome c/Apaf-1/dATP complex, thereby inhibiting the activation of procaspase-9. It is also hypothesized that HSP27 may serve some role in cross-bridge formation between actin and myosin (5). And finally, HSP27 is also thought to be involved in the process of cell differentiation. The up-regulation of HSP27 correlates with the rate of phosphorylation and with an increase of large oligomers. It is possible that HSP27 may play a crucial role in termination of growth (6). Looking for more information on HSP27? Visit our new HSP27 Scientific Resource Guide at http://www.HSP27.com.
This product has been certified >90% pure using SDS-PAGE analysis.
Cellular Localization:
Cytoplasm | Nucleus
References:
1. Kim K.K., Kim R., and Kim, S. (1998) Nature 394(6693): 595-599. 2. Van Montfort R., Slingsby C., and Vierling E. (2001) Addv Protein Chem. 59: 105-56. 3. Ehrnsperger M., Graber S., Gaestel M. and Buchner J. (1997) EMBO J. 16: 221-229. 4. Ciocca D.R., Oesterreich S., Chamness G.C., McGuire W.L., and Fugua S.A. (1993) J Natl Cancer Inst. 85 (19): 1558-70. 5. Sarto C. Binnz P.A. and Mocarelli P. (2000) Electrophoresis. 21(6): 1218-26. 6. Arrigo A.P. (2005) J Cell Biochem. 94(2): 241-6.
HSP27s belong to an abundant and ubiquitous family of small heat shock proteins (sHSP). It is an important HSP found in both normal human cells and cancer cells. The basic structure of most sHSPs is a homologous and highly conserved amino acid sequence, with an ?-crystallin-domain at the C-terminus and the WD/EPF domain at the less conserved N-terminus. This N-terminus is essential for the development of high molecular oligomers (1, 2). HSP27-oligomers consist of stable dimers formed by as many as 8-40 HSP27 protein monomers (3). The oligomerization status is connected with the chaperone activity: aggregates of large oligomers have high chaperone activity, whereas dimers have no chaperone activity (4). HSP27 is localized to the cytoplasm of unstressed cells but can redistribute to the nucleus in response to stress, where it may function to stabilize DNA and/or the nuclear membrane. Other functions include chaperone activity (as mentioned above), thermo tolerance in vivo, inhibition of apoptosis, and signal transduction. Specifically, in vitro, it acts as an ATP-independent chaperone by inhibiting protein aggregation and by stabilizing partially denatured proteins, which ensures refolding of the HSP70 complex. HSP27 is also involved in the apoptotic signaling pathway because it interferes with the activation of cytochrome c/Apaf-1/dATP complex, thereby inhibiting the activation of procaspase-9. It is also hypothesized that HSP27 may serve some role in cross-bridge formation between actin and myosin (5). And finally, HSP27 is also thought to be involved in the process of cell differentiation. The up-regulation of HSP27 correlates with the rate of phosphorylation and with an increase of large oligomers. It is possible that HSP27 may play a crucial role in termination of growth (6). Looking for more information on HSP27? Visit our new HSP27 Scientific Resource Guide at http://www.HSP27.com.
This product has been certified >90% pure using SDS-PAGE analysis.
Cellular Localization:
Cytoplasm | Nucleus
References:
1. Kim K.K., Kim R., and Kim, S. (1998) Nature 394(6693): 595-599. 2. Van Montfort R., Slingsby C., and Vierling E. (2001) Addv Protein Chem. 59: 105-56. 3. Ehrnsperger M., Graber S., Gaestel M. and Buchner J. (1997) EMBO J. 16: 221-229. 4. Ciocca D.R., Oesterreich S., Chamness G.C., McGuire W.L., and Fugua S.A. (1993) J Natl Cancer Inst. 85 (19): 1558-70. 5. Sarto C. Binnz P.A. and Mocarelli P. (2000) Electrophoresis. 21(6): 1218-26. 6. Arrigo A.P. (2005) J Cell Biochem. 94(2): 241-6.
GRP78 is a ubiquitously expressed, 78-kDa glucose-regulated protein, and is commonly referred to as an immunoglobin chain binding protein (BiP). The BiP proteins are categorized as stress response proteins because they play an important role in the proper folding and assembly of nascent protein and in the scavenging of misfolded proteins in the endoplasmic reticulum lumen. Translation of BiP is directed by an internal ribosomal entry site (IRES) in the 5' non-translated region of the BiP mRNA. BiP IRES activity increases when cells are heat stressed (1). GRP78 is also critical for maintenance of cell homeostasis and the prevention of apoptosis (2). Luo et al. have provided findings that suggest GRP78 is essential for embryonic cell growth and pluripotent cell survival (3). In terms of diseases, GRP78 has been shown to be a reliable biomarker of hypoglycemia (Barnes), to serve a neuroprotective function in neurons exposed to glutamate and oxidative stress (4), and its protein levels are reduced in the brains of Alzheimer's patients (5). Also, the induction of the GRP78 protein that results in severe glucose and oxygen deprivation could possible lead to drug resistance to anti-tumor drugs (6, 7).
Cancer | Heat Shock | Cell Signaling | Protein Trafficking | Chaperone Proteins | Organelle Markers
Alternative Name(s):
BIP Protein, Grp78 Protein, HSPA5 Protein, MIF2 Protein, immunoglobulin heavy chain binding Protein
Category:
Recombinant
Accession Number:
NM_005347
Gene ID:
3309
Swiss-Prot:
P11021
Purification:
Affinity Purified
Concentration:
Lot/batch specific. See included datasheet.
Specificity:
~78 kDa
Certificate of Analysis:
This product has been certified >90% pure using SDS-PAGE analysis and gamma globulin as the protein concentration standard.
Cellular Localization:
Endoplasmic Reticulum Lumen | Melanosome
References:
1. Cho S., et al (2007) Mol Cell Biol. 27(1): 368-83. 2. Yang Y., et al. (1998) J Biol Chem. 273: 25552-25555. 3. Luo S., et al (2006) 26(15): 5688-97. 4. Yu Z., et al. (1999) Exp Neurol. 15: 302-314. 5. Koomagi R., et al. (1999) Anticancer Res. 19: 4333-4336. 6. Laquerre S., et al. (1998) J. Virology. 72: 4940-4949. 7. Dong D., et al. (2005) Cancer Res. 65(13): 5785-91.
GRP78 is a ubiquitously expressed, 78-kDa glucose-regulated protein, and is commonly referred to as an immunoglobin chain binding protein (BiP). The BiP proteins are categorized as stress response proteins because they play an important role in the proper folding and assembly of nascent protein and in the scavenging of misfolded proteins in the endoplasmic reticulum lumen. Translation of BiP is directed by an internal ribosomal entry site (IRES) in the 5' non-translated region of the BiP mRNA. BiP IRES activity increases when cells are heat stressed (1). GRP78 is also critical for maintenance of cell homeostasis and the prevention of apoptosis (2). Luo et al. have provided findings that suggest GRP78 is essential for embryonic cell growth and pluripotent cell survival (3). In terms of diseases, GRP78 has been shown to be a reliable biomarker of hypoglycemia (Barnes), to serve a neuroprotective function in neurons exposed to glutamate and oxidative stress (4), and its protein levels are reduced in the brains of Alzheimer's patients (5). Also, the induction of the GRP78 protein that results in severe glucose and oxygen deprivation could possible lead to drug resistance to anti-tumor drugs (6, 7).
Cancer | Heat Shock | Cell Signaling | Protein Trafficking | Chaperone Proteins | Organelle Markers
Alternative Name(s):
BIP Protein, Grp78 Protein, HSPA5 Protein, MIF2 Protein, immunoglobulin heavy chain binding Protein
Category:
Recombinant
Accession Number:
NM_005347
Gene ID:
3309
Swiss-Prot:
P11021
Purification:
Affinity Purified
Concentration:
Lot/batch specific. See included datasheet.
Specificity:
~78 kDa
Certificate of Analysis:
This product has been certified >90% pure using SDS-PAGE analysis and gamma globulin as the protein concentration standard.
Cellular Localization:
Endoplasmic Reticulum Lumen | Melanosome
References:
1. Cho S., et al (2007) Mol Cell Biol. 27(1): 368-83. 2. Yang Y., et al. (1998) J Biol Chem. 273: 25552-25555. 3. Luo S., et al (2006) 26(15): 5688-97. 4. Yu Z., et al. (1999) Exp Neurol. 15: 302-314. 5. Koomagi R., et al. (1999) Anticancer Res. 19: 4333-4336. 6. Laquerre S., et al. (1998) J. Virology. 72: 4940-4949. 7. Dong D., et al. (2005) Cancer Res. 65(13): 5785-91.
GRP78 is a ubiquitously expressed, 78-kDa glucose-regulated protein, and is commonly referred to as an immunoglobin chain binding protein (BiP). The BiP proteins are categorized as stress response proteins because they play an important role in the proper folding and assembly of nascent protein and in the scavenging of misfolded proteins in the endoplasmic reticulum lumen. Translation of BiP is directed by an internal ribosomal entry site (IRES) in the 5' non-translated region of the BiP mRNA. BiP IRES activity increases when cells are heat stressed (1). GRP78 is also critical for maintenance of cell homeostasis and the prevention of apoptosis (2). Luo et al. have provided findings that suggest GRP78 is essential for embryonic cell growth and pluripotent cell survival (3). In terms of diseases, GRP78 has been shown to be a reliable biomarker of hypoglycemia (Barnes), to serve a neuroprotective function in neurons exposed to glutamate and oxidative stress (4), and its protein levels are reduced in the brains of Alzheimer's patients (5). Also, the induction of the GRP78 protein that results in severe glucose and oxygen deprivation could possible lead to drug resistance to anti-tumor drugs (6, 7).
Cancer | Heat Shock | Cell Signaling | Protein Trafficking | Chaperone Proteins | Organelle Markers
Alternative Name(s):
BIP Protein, Grp78 Protein, HSPA5 Protein, MIF2 Protein, immunoglobulin heavy chain binding Protein
Category:
Recombinant
Accession Number:
NM_005347
Gene ID:
3309
Swiss-Prot:
P11021
Purification:
Affinity Purified
Concentration:
Lot/batch specific. See included datasheet.
Specificity:
~78 kDa
Certificate of Analysis:
This product has been certified >90% pure using SDS-PAGE analysis and gamma globulin as the protein concentration standard.
Cellular Localization:
Endoplasmic Reticulum Lumen | Melanosome
References:
1. Cho S., et al (2007) Mol Cell Biol. 27(1): 368-83. 2. Yang Y., et al. (1998) J Biol Chem. 273: 25552-25555. 3. Luo S., et al (2006) 26(15): 5688-97. 4. Yu Z., et al. (1999) Exp Neurol. 15: 302-314. 5. Koomagi R., et al. (1999) Anticancer Res. 19: 4333-4336. 6. Laquerre S., et al. (1998) J. Virology. 72: 4940-4949. 7. Dong D., et al. (2005) Cancer Res. 65(13): 5785-91.
Rab5 is a 24kDa member of the Rab family of small guanosine triphosphatases (GTPases), Ras superfamily. Rab GTPases are central regulators of membrane trafficking in the eukaryotic cell. Their regulatory capacity depends on their ability to cycle between the GDP -bound inactive and GTP-bound active states. This conversion is regulated by GDP/GTP exchange factors (GEPs), GDP dissociation inhibitors (GDIs) and GTPase-activating proteins (GAPs) (1, 2). Activation of a Rab protein is coupled to its association with intracellular membranes, allowing it to recruit downstream effector proteins to the cytoplasmic surface of a subcellular compartment (3). Through these proteins, Rab GTPases regulate vesicle formation, actin- and tubulin-dependent vesicle movement, and membrane fusion(1). Rab proteins contain conserved regions involved in guanine-nucleotide binding, and hyper variable COHO-terminal domains with a cysteine motif implicated in subcellular targeting. Post-translational modification of the cysteine motif with one or two geranyl groups is essential for the membrane association and correct intracellular localization of Rab proteins(3). Each Rab shows a characteristic subcellular distribution (4). In particular, Rab5 is ubiquitously expressed in human tissues. It localizes mainly to early endosomes, but is also present on the plasma membrane. It regulates the fusion between endocytic vesicles and early endosomes, as well as the homotypic fusion between early endosomes (5). Among the proteins recruited by the GTP-bound active Rab5 are Rabaptin-5 and EEA1 (6). Anti-Rab5 may be used as an early endosome marker.
Rab5 is a 24kDa member of the Rab family of small guanosine triphosphatases (GTPases), Ras superfamily. Rab GTPases are central regulators of membrane trafficking in the eukaryotic cell. Their regulatory capacity depends on their ability to cycle between the GDP -bound inactive and GTP-bound active states. This conversion is regulated by GDP/GTP exchange factors (GEPs), GDP dissociation inhibitors (GDIs) and GTPase-activating proteins (GAPs) (1, 2). Activation of a Rab protein is coupled to its association with intracellular membranes, allowing it to recruit downstream effector proteins to the cytoplasmic surface of a subcellular compartment (3). Through these proteins, Rab GTPases regulate vesicle formation, actin- and tubulin-dependent vesicle movement, and membrane fusion(1). Rab proteins contain conserved regions involved in guanine-nucleotide binding, and hyper variable COHO-terminal domains with a cysteine motif implicated in subcellular targeting. Post-translational modification of the cysteine motif with one or two geranyl groups is essential for the membrane association and correct intracellular localization of Rab proteins(3). Each Rab shows a characteristic subcellular distribution (4). In particular, Rab5 is ubiquitously expressed in human tissues. It localizes mainly to early endosomes, but is also present on the plasma membrane. It regulates the fusion between endocytic vesicles and early endosomes, as well as the homotypic fusion between early endosomes (5). Among the proteins recruited by the GTP-bound active Rab5 are Rabaptin-5 and EEA1 (6). Anti-Rab5 may be used as an early endosome marker.
Product Type:
Protein
Format:
20mM Tris/HCl, pH7.5, 0.15M NaCl
Storage Temp:
-20ºC
Applications:
WB | SDS-PAGE
Target:
Rab5
Conjugate:
His tag
Research Area(s):
Cancer | Heat Shock
Alternative Name(s):
Rab 5A Protein, RAS associated protein RAB5A Protein, Ras related protein Rab 5 A Protein
Category:
Recombinant
Accession Number:
BC001267
Gene ID:
5868
Swiss-Prot:
P20339
Purification:
Affinity Purified
Concentration:
Lot/batch specific. See included datasheet.
Specificity:
~26 kDa
Certificate of Analysis:
This product has been certified >90% pure using SDS-PAGE analysis.
Cellular Localization:
Cell Membrane | Early Endosome Membrane | Melanosome
References:
1. Stenmark H., and Olkkonen V.M. (2001) Genome Biol. 2: 3007.1-3007.7. 2. Takai Y., et al. (2001) Physiol. Rev. 8:, 153-208. 3. Ali B.R., et al. (2004) J. Cell Sci. 117: 6401-6412. 4. Zerial M., and McBride H. (2001) Nat. Rev. Mol. Cell Biol. 2: 107-117. 5. Sonnichsen B., et al. (2000) J. Cell Biol. 149: 901-913 6. Woodman P.G. (2000) Traffic. 1: 695-701.
Rab5 is a 24kDa member of the Rab family of small guanosine triphosphatases (GTPases), Ras superfamily. Rab GTPases are central regulators of membrane trafficking in the eukaryotic cell. Their regulatory capacity depends on their ability to cycle between the GDP -bound inactive and GTP-bound active states. This conversion is regulated by GDP/GTP exchange factors (GEPs), GDP dissociation inhibitors (GDIs) and GTPase-activating proteins (GAPs) (1, 2). Activation of a Rab protein is coupled to its association with intracellular membranes, allowing it to recruit downstream effector proteins to the cytoplasmic surface of a subcellular compartment (3). Through these proteins, Rab GTPases regulate vesicle formation, actin- and tubulin-dependent vesicle movement, and membrane fusion(1). Rab proteins contain conserved regions involved in guanine-nucleotide binding, and hyper variable COHO-terminal domains with a cysteine motif implicated in subcellular targeting. Post-translational modification of the cysteine motif with one or two geranyl groups is essential for the membrane association and correct intracellular localization of Rab proteins(3). Each Rab shows a characteristic subcellular distribution (4). In particular, Rab5 is ubiquitously expressed in human tissues. It localizes mainly to early endosomes, but is also present on the plasma membrane. It regulates the fusion between endocytic vesicles and early endosomes, as well as the homotypic fusion between early endosomes (5). Among the proteins recruited by the GTP-bound active Rab5 are Rabaptin-5 and EEA1 (6). Anti-Rab5 may be used as an early endosome marker.
Product Type:
Protein
Format:
20mM Tris/HCl, pH7.5, 0.15M NaCl
Storage Temp:
-20ºC
Applications:
WB | SDS-PAGE
Target:
Rab5
Conjugate:
His tag
Research Area(s):
Cancer | Heat Shock
Alternative Name(s):
Rab 5A Protein, RAS associated protein RAB5A Protein, Ras related protein Rab 5 A Protein
Category:
Recombinant
Accession Number:
BC001267
Gene ID:
5868
Swiss-Prot:
P20339
Purification:
Affinity Purified
Concentration:
Lot/batch specific. See included datasheet.
Specificity:
~26 kDa
Certificate of Analysis:
This product has been certified >90% pure using SDS-PAGE analysis.
Cellular Localization:
Cell Membrane | Early Endosome Membrane | Melanosome
References:
1. Stenmark H., and Olkkonen V.M. (2001) Genome Biol. 2: 3007.1-3007.7. 2. Takai Y., et al. (2001) Physiol. Rev. 8:, 153-208. 3. Ali B.R., et al. (2004) J. Cell Sci. 117: 6401-6412. 4. Zerial M., and McBride H. (2001) Nat. Rev. Mol. Cell Biol. 2: 107-117. 5. Sonnichsen B., et al. (2000) J. Cell Biol. 149: 901-913 6. Woodman P.G. (2000) Traffic. 1: 695-701.
HSP90 is an abundantly and ubiquitously expressed heat shock protein. It is understood to exist in two principal forms alpha and beta, which share 85% sequence amino acid homology. The two isoforms of HSP90 are expressed in the cytosolic compartment (1). Despite the similarities, HSP90alpha exists predominantly as a homodimer while HSP90beta exists mainly as a monomer (2). From a functional perspective, HSP90 participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex (3-6). Furthermore, HSP90 is highly conserved between species; having 60% and 78% amino acid similarity between mammalian and the corresponding yeast and Drosophila proteins, respectively. HSP90 is a highly conserved and essential stress protein that is expressed in all eukaryotic cells. Despite its label of being a heat-shock protein, HSP90 is one of the most highly expressed proteins in unstressed cells (1-2% of cytosolic protein). It carries out a number of housekeeping functions, including controlling the activity, turnover, and trafficking of a variety of proteins. Most of the HSP90-regulated proteins that have been discovered to date are involved in cell signaling (7-8). The number of proteins now know to interact with HSP90 is about 100. Target proteins include the kinases v-Src, Wee1, and c-Raf, transcriptional regulators such as p53 and steroid receptors, and the polymerases of the hepatitis B virus and telomerase (5). When bound to ATP, HSP90 interacts with co-chaperones Cdc37, p23, and an assortment of immunophilin-like proteins, forming a complex that stabilizes and protects target proteins from proteasomal degradation. In most cases, HSP90-interacting proteins have been shown to co-precipitate with HSP90 when carrying out immune adsorption studies, and to exist in cytosolic heterocomplexes with it. In a number of cases, variations in HSP90 expression or HSP90 mutation has been shown to degrade signaling function via the protein or to impair a specific function of the protein (such as steroid binding, kinase activity) in vivo. Ansamycin antibiotics, such as geldanamycin and radicicol, inhibit HSP90 function (9). Recently, Prof. Tatu's laboratory has shown the importance of HSP90 in parasite growth. They have shown that inhibition of P. Falciparum HSP90 (PfHSP90), blocks the erythrocytic cycle by inhibiting stage transformation, leading to inhibition of parasite growth (10, 11). Looking for more information on HSP90? Visit our new HSP90 Scientific Resource Guide at http://www.HSP90.ca.
Product Type:
Protein
Format:
50mM Tris/HCl pH7.5, 300mM NaCl, 10% glycerol
Storage Temp:
-20ºC
Applications:
WB | SDS-PAGE
Target:
HSP90
Conjugate:
No tag
Research Area(s):
Cancer | Heat Shock | Cell Signaling | Protein Trafficking | Chaperone Proteins | Cancer | Tumor Biomarkers
Alternative Name(s):
PfHSP90 Protein, Pf14_-417 HSP90 Protein, HSP90 Protein
Category:
Recombinant
Accession Number:
XP_001348591.1
Gene ID:
811999
Swiss-Prot:
Q8IL32
Purification:
Affinity Purified
Concentration:
Lot/batch specific. See included datasheet.
Specificity:
~21.4 kDa
Certificate of Analysis:
This product has been certified >90% pure using SDS-PAGE analysis.
Cellular Localization:
Cytoplasm | Melanosome
References:
1. Nemoto T., et al. (1997) J.Biol Chem. 272: 26179-26187. 2. Minami Y., et al. (1991) J.Biol Chem. 266: 10099-10103. 3. Arlander S.J.H, et al. (2003) J Biol Chem. 278: 52572-52577. 4. Pearl H., et al. (2001) Adv Protein Chem. 59: 157-186. 5. Neckers L., et al. (2002) Trends Mol Med. 8: S55-S61. 6. Pratt W., Toft D. (2003) Exp Biol Med. 228: 111-133. 7. Pratt W., Toft D. (1997) Endocr Rev. 18: 306360. 8. Pratt W.B. (1998) Proc Soc Exptl Biol Med. 217: 420434. 9. Whitesell L., et al. (1994) Proc Natl Acad Sci USA. 91: 83248328. 10. Banumathy G., Singh V., Pavithra S.R., and Tatu U. (2003) J Biol Chem. 278(20): 18336-45. 11. Pavithra S.R, Banumathy G., Joy O., Singh V., and Tatu U. (2004) J Biol Chem. 279(45): 46692-9.
HSP90 is an abundantly and ubiquitously expressed heat shock protein. It is understood to exist in two principal forms alpha and beta, which share 85% sequence amino acid homology. The two isoforms of HSP90 are expressed in the cytosolic compartment (1). Despite the similarities, HSP90alpha exists predominantly as a homodimer while HSP90beta exists mainly as a monomer (2). From a functional perspective, HSP90 participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex (3-6). Furthermore, HSP90 is highly conserved between species; having 60% and 78% amino acid similarity between mammalian and the corresponding yeast and Drosophila proteins, respectively. HSP90 is a highly conserved and essential stress protein that is expressed in all eukaryotic cells. Despite its label of being a heat-shock protein, HSP90 is one of the most highly expressed proteins in unstressed cells (1-2% of cytosolic protein). It carries out a number of housekeeping functions, including controlling the activity, turnover, and trafficking of a variety of proteins. Most of the HSP90-regulated proteins that have been discovered to date are involved in cell signaling (7-8). The number of proteins now know to interact with HSP90 is about 100. Target proteins include the kinases v-Src, Wee1, and c-Raf, transcriptional regulators such as p53 and steroid receptors, and the polymerases of the hepatitis B virus and telomerase (5). When bound to ATP, HSP90 interacts with co-chaperones Cdc37, p23, and an assortment of immunophilin-like proteins, forming a complex that stabilizes and protects target proteins from proteasomal degradation. In most cases, HSP90-interacting proteins have been shown to co-precipitate with HSP90 when carrying out immune adsorption studies, and to exist in cytosolic heterocomplexes with it. In a number of cases, variations in HSP90 expression or HSP90 mutation has been shown to degrade signaling function via the protein or to impair a specific function of the protein (such as steroid binding, kinase activity) in vivo. Ansamycin antibiotics, such as geldanamycin and radicicol, inhibit HSP90 function (9). Recently, Prof. Tatu's laboratory has shown the importance of HSP90 in parasite growth. They have shown that inhibition of P. Falciparum HSP90 (PfHSP90), blocks the erythrocytic cycle by inhibiting stage transformation, leading to inhibition of parasite growth (10, 11). Looking for more information on HSP90? Visit our new HSP90 Scientific Resource Guide at http://www.HSP90.ca.
Product Type:
Protein
Format:
50mM Tris/HCl pH7.5, 300mM NaCl, 10% glycerol
Storage Temp:
-20ºC
Applications:
WB | SDS-PAGE
Target:
HSP90
Conjugate:
No tag
Research Area(s):
Cancer | Heat Shock | Cell Signaling | Protein Trafficking | Chaperone Proteins | Cancer | Tumor Biomarkers
Alternative Name(s):
PfHSP90 Protein, Pf14_-417 HSP90 Protein, HSP90 Protein
Category:
Recombinant
Accession Number:
XP_001348591.1
Gene ID:
811999
Swiss-Prot:
Q8IL32
Purification:
Affinity Purified
Concentration:
Lot/batch specific. See included datasheet.
Specificity:
~21.4 kDa
Certificate of Analysis:
This product has been certified >90% pure using SDS-PAGE analysis.
Cellular Localization:
Cytoplasm | Melanosome
References:
1. Nemoto T., et al. (1997) J.Biol Chem. 272: 26179-26187. 2. Minami Y., et al. (1991) J.Biol Chem. 266: 10099-10103. 3. Arlander S.J.H, et al. (2003) J Biol Chem. 278: 52572-52577. 4. Pearl H., et al. (2001) Adv Protein Chem. 59: 157-186. 5. Neckers L., et al. (2002) Trends Mol Med. 8: S55-S61. 6. Pratt W., Toft D. (2003) Exp Biol Med. 228: 111-133. 7. Pratt W., Toft D. (1997) Endocr Rev. 18: 306360. 8. Pratt W.B. (1998) Proc Soc Exptl Biol Med. 217: 420434. 9. Whitesell L., et al. (1994) Proc Natl Acad Sci USA. 91: 83248328. 10. Banumathy G., Singh V., Pavithra S.R., and Tatu U. (2003) J Biol Chem. 278(20): 18336-45. 11. Pavithra S.R, Banumathy G., Joy O., Singh V., and Tatu U. (2004) J Biol Chem. 279(45): 46692-9.
HSP90 is an abundantly and ubiquitously expressed heat shock protein. It is understood to exist in two principal forms alpha and beta, which share 85% sequence amino acid homology. The two isoforms of HSP90 are expressed in the cytosolic compartment (1). Despite the similarities, HSP90alpha exists predominantly as a homodimer while HSP90beta exists mainly as a monomer (2). From a functional perspective, HSP90 participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex (3-6). Furthermore, HSP90 is highly conserved between species; having 60% and 78% amino acid similarity between mammalian and the corresponding yeast and Drosophila proteins, respectively. HSP90 is a highly conserved and essential stress protein that is expressed in all eukaryotic cells. Despite its label of being a heat-shock protein, HSP90 is one of the most highly expressed proteins in unstressed cells (1-2% of cytosolic protein). It carries out a number of housekeeping functions, including controlling the activity, turnover, and trafficking of a variety of proteins. Most of the HSP90-regulated proteins that have been discovered to date are involved in cell signaling (7-8). The number of proteins now know to interact with HSP90 is about 100. Target proteins include the kinases v-Src, Wee1, and c-Raf, transcriptional regulators such as p53 and steroid receptors, and the polymerases of the hepatitis B virus and telomerase (5). When bound to ATP, HSP90 interacts with co-chaperones Cdc37, p23, and an assortment of immunophilin-like proteins, forming a complex that stabilizes and protects target proteins from proteasomal degradation. In most cases, HSP90-interacting proteins have been shown to co-precipitate with HSP90 when carrying out immune adsorption studies, and to exist in cytosolic heterocomplexes with it. In a number of cases, variations in HSP90 expression or HSP90 mutation has been shown to degrade signaling function via the protein or to impair a specific function of the protein (such as steroid binding, kinase activity) in vivo. Ansamycin antibiotics, such as geldanamycin and radicicol, inhibit HSP90 function (9). Recently, Prof. Tatu's laboratory has shown the importance of HSP90 in parasite growth. They have shown that inhibition of P. Falciparum HSP90 (PfHSP90), blocks the erythrocytic cycle by inhibiting stage transformation, leading to inhibition of parasite growth (10, 11). Looking for more information on HSP90? Visit our new HSP90 Scientific Resource Guide at http://www.HSP90.ca.
Product Type:
Protein
Format:
50mM Tris/HCl pH7.5, 300mM NaCl, 10% glycerol
Storage Temp:
-20ºC
Applications:
WB | SDS-PAGE
Target:
HSP90
Conjugate:
No tag
Research Area(s):
Cancer | Heat Shock | Cell Signaling | Protein Trafficking | Chaperone Proteins | Cancer | Tumor Biomarkers
Alternative Name(s):
PfHSP90 Protein, Pf14_-417 HSP90 Protein, HSP90 Protein
Category:
Recombinant
Accession Number:
XP_001348591.1
Gene ID:
811999
Swiss-Prot:
Q8IL32
Purification:
Affinity Purified
Concentration:
Lot/batch specific. See included datasheet.
Specificity:
~21.4 kDa
Certificate of Analysis:
This product has been certified >90% pure using SDS-PAGE analysis.
Cellular Localization:
Cytoplasm | Melanosome
References:
1. Nemoto T., et al. (1997) J.Biol Chem. 272: 26179-26187. 2. Minami Y., et al. (1991) J.Biol Chem. 266: 10099-10103. 3. Arlander S.J.H, et al. (2003) J Biol Chem. 278: 52572-52577. 4. Pearl H., et al. (2001) Adv Protein Chem. 59: 157-186. 5. Neckers L., et al. (2002) Trends Mol Med. 8: S55-S61. 6. Pratt W., Toft D. (2003) Exp Biol Med. 228: 111-133. 7. Pratt W., Toft D. (1997) Endocr Rev. 18: 306360. 8. Pratt W.B. (1998) Proc Soc Exptl Biol Med. 217: 420434. 9. Whitesell L., et al. (1994) Proc Natl Acad Sci USA. 91: 83248328. 10. Banumathy G., Singh V., Pavithra S.R., and Tatu U. (2003) J Biol Chem. 278(20): 18336-45. 11. Pavithra S.R, Banumathy G., Joy O., Singh V., and Tatu U. (2004) J Biol Chem. 279(45): 46692-9.
Superoxide dismutase (SOD) is an endogenously produced intracellular enzyme present in almost every cell in the body (3). It works by catalyzing the dismutation of the superoxide radical O2? to O2 and H2O2, which are then metabolized to H2O and O2 by catalase and glutathione peroxidase (2, 5). In general, SODs play a major role in antioxidant defense mechanisms (4). There are two main types of SOD in mammalian cells. One form (SOD1) contains Cu and Zn ions as a homodimer and exists in the cytoplasm. The two subunits of 16 kDa each are linked by two cysteines forming an intra-subunit disulphide bridge (3). The second form (SOD2) is a manganese containing enzyme and resides in the mitochondrial matrix. It is a homotetramer of 80 kDa. The third form (SOD3 or EC-SOD) is like SOD1 in that it contains Cu and Zn ions, however it is distinct in that it is a homotetramer, with a mass of 30 kDA and it exists only in the extracellular space(8). SOD3 can also be distinguished by its heparin-binding capacity (1).
Product Type:
Protein
Format:
50mM Tris/HCl pH7.7, 0.3M NaCl
Storage Temp:
-20ºC
Applications:
WB | SDS-PAGE
Target:
Mn SOD
Conjugate:
His tag
Research Area(s):
Cancer | Oxidative Stress | Cell Signaling | Protein Trafficking | Chaperone Proteins
Alternative Name(s):
Manganese SOD Protein, IPO B Protein, Mn SOD Protein, SOD2 Protein
Category:
Recombinant
Accession Number:
BC070913
Gene ID:
24787
Swiss-Prot:
P07895
Purification:
Affinity Purified
Concentration:
Lot/batch specific. See included datasheet.
Specificity:
~25 kDa
Certificate of Analysis:
This product has been certified >90% pure using SDS-PAGE analysis.
Cellular Localization:
Mitochondrion Matrix
References:
1. Adachi T., et al. (1992) Clin. Chim. Acta. 212: 89-102. 2. Barrister J.V., et al. (1987) Crit. Rev. Biochem. 22: 111-180. 3. Furukawa Y., and O'Halloran T. (2006) Antioxidants &Redo Signaling. 8 (No 5): 6. 4. Gao B., et al. (2003). Am J Physiol Lung Cell Mol Physiol. 284: L917-L925. 5. Hassan H.M. (1988). Free Radical Biol. Med. 5: 377-385. 6. Kurobe N., et al. (1990) Clinica Chimica Acta. 192: 171-180. 7. Ojika T., et al. (1991) Acta Histochem Cytochem. 24(50): 489-495. 8. Wispe J.R., et al. (1989) BBA. 994: 30-36.
Superoxide dismutase (SOD) is an endogenously produced intracellular enzyme present in almost every cell in the body (3). It works by catalyzing the dismutation of the superoxide radical O2? to O2 and H2O2, which are then metabolized to H2O and O2 by catalase and glutathione peroxidase (2, 5). In general, SODs play a major role in antioxidant defense mechanisms (4). There are two main types of SOD in mammalian cells. One form (SOD1) contains Cu and Zn ions as a homodimer and exists in the cytoplasm. The two subunits of 16 kDa each are linked by two cysteines forming an intra-subunit disulphide bridge (3). The second form (SOD2) is a manganese containing enzyme and resides in the mitochondrial matrix. It is a homotetramer of 80 kDa. The third form (SOD3 or EC-SOD) is like SOD1 in that it contains Cu and Zn ions, however it is distinct in that it is a homotetramer, with a mass of 30 kDA and it exists only in the extracellular space(8). SOD3 can also be distinguished by its heparin-binding capacity (1).
Product Type:
Protein
Format:
50mM Tris/HCl pH7.7, 0.3M NaCl
Storage Temp:
-20ºC
Applications:
WB | SDS-PAGE
Target:
Mn SOD
Conjugate:
His tag
Research Area(s):
Cancer | Oxidative Stress | Cell Signaling | Protein Trafficking | Chaperone Proteins
Alternative Name(s):
Manganese SOD Protein, IPO B Protein, Mn SOD Protein, SOD2 Protein
Category:
Recombinant
Accession Number:
BC070913
Gene ID:
24787
Swiss-Prot:
P07895
Purification:
Affinity Purified
Concentration:
Lot/batch specific. See included datasheet.
Specificity:
~25 kDa
Certificate of Analysis:
This product has been certified >90% pure using SDS-PAGE analysis.
Cellular Localization:
Mitochondrion Matrix
References:
1. Adachi T., et al. (1992) Clin. Chim. Acta. 212: 89-102. 2. Barrister J.V., et al. (1987) Crit. Rev. Biochem. 22: 111-180. 3. Furukawa Y., and O'Halloran T. (2006) Antioxidants &Redo Signaling. 8 (No 5): 6. 4. Gao B., et al. (2003). Am J Physiol Lung Cell Mol Physiol. 284: L917-L925. 5. Hassan H.M. (1988). Free Radical Biol. Med. 5: 377-385. 6. Kurobe N., et al. (1990) Clinica Chimica Acta. 192: 171-180. 7. Ojika T., et al. (1991) Acta Histochem Cytochem. 24(50): 489-495. 8. Wispe J.R., et al. (1989) BBA. 994: 30-36.
Superoxide dismutase (SOD) is an endogenously produced intracellular enzyme present in almost every cell in the body (3). It works by catalyzing the dismutation of the superoxide radical O2? to O2 and H2O2, which are then metabolized to H2O and O2 by catalase and glutathione peroxidase (2, 5). In general, SODs play a major role in antioxidant defense mechanisms (4). There are two main types of SOD in mammalian cells. One form (SOD1) contains Cu and Zn ions as a homodimer and exists in the cytoplasm. The two subunits of 16 kDa each are linked by two cysteines forming an intra-subunit disulphide bridge (3). The second form (SOD2) is a manganese containing enzyme and resides in the mitochondrial matrix. It is a homotetramer of 80 kDa. The third form (SOD3 or EC-SOD) is like SOD1 in that it contains Cu and Zn ions, however it is distinct in that it is a homotetramer, with a mass of 30 kDA and it exists only in the extracellular space(8). SOD3 can also be distinguished by its heparin-binding capacity (1).
Product Type:
Protein
Format:
50mM Tris/HCl pH7.7, 0.3M NaCl
Storage Temp:
-20ºC
Applications:
WB | SDS-PAGE
Target:
Mn SOD
Conjugate:
His tag
Research Area(s):
Cancer | Oxidative Stress | Cell Signaling | Protein Trafficking | Chaperone Proteins
Alternative Name(s):
Manganese SOD Protein, IPO B Protein, Mn SOD Protein, SOD2 Protein
Category:
Recombinant
Accession Number:
BC070913
Gene ID:
24787
Swiss-Prot:
P07895
Purification:
Affinity Purified
Concentration:
Lot/batch specific. See included datasheet.
Specificity:
~25 kDa
Certificate of Analysis:
This product has been certified >90% pure using SDS-PAGE analysis.
Cellular Localization:
Mitochondrion Matrix
References:
1. Adachi T., et al. (1992) Clin. Chim. Acta. 212: 89-102. 2. Barrister J.V., et al. (1987) Crit. Rev. Biochem. 22: 111-180. 3. Furukawa Y., and O'Halloran T. (2006) Antioxidants &Redo Signaling. 8 (No 5): 6. 4. Gao B., et al. (2003). Am J Physiol Lung Cell Mol Physiol. 284: L917-L925. 5. Hassan H.M. (1988). Free Radical Biol. Med. 5: 377-385. 6. Kurobe N., et al. (1990) Clinica Chimica Acta. 192: 171-180. 7. Ojika T., et al. (1991) Acta Histochem Cytochem. 24(50): 489-495. 8. Wispe J.R., et al. (1989) BBA. 994: 30-36.
Superoxide dismutase (SOD) is an endogenously produced intracellular enzyme present in almost every cell in the body (3). It works by catalyzing the dismutation of the superoxide radical O2? to O2 and H2O2, which are then metabolized to H2O and O2 by catalase and glutathione peroxidase (2, 5). In general, SODs play a major role in antioxidant defense mechanisms (4). There are two main types of SOD in mammalian cells. One form (SOD1) contains Cu and Zn ions as a homodimer and exists in the cytoplasm. The two subunits of 16 kDa each are linked by two cysteines forming an intra-subunit disulphide bridge (3). The second form (SOD2) is a manganese containing enzyme and resides in the mitochondrial matrix. It is a homotetramer of 80 kDa. The third form (SOD3 or EC-SOD) is like SOD1 in that it contains Cu and Zn ions, however it is distinct in that it is a homotetramer, with a mass of 30 kDA and it exists only in the extracellular space(8). SOD3 can also be distinguished by its heparin-binding capacity (1).
Superoxide dismutase (SOD) is an endogenously produced intracellular enzyme present in almost every cell in the body (3). It works by catalyzing the dismutation of the superoxide radical O2? to O2 and H2O2, which are then metabolized to H2O and O2 by catalase and glutathione peroxidase (2, 5). In general, SODs play a major role in antioxidant defense mechanisms (4). There are two main types of SOD in mammalian cells. One form (SOD1) contains Cu and Zn ions as a homodimer and exists in the cytoplasm. The two subunits of 16 kDa each are linked by two cysteines forming an intra-subunit disulphide bridge (3). The second form (SOD2) is a manganese containing enzyme and resides in the mitochondrial matrix. It is a homotetramer of 80 kDa. The third form (SOD3 or EC-SOD) is like SOD1 in that it contains Cu and Zn ions, however it is distinct in that it is a homotetramer, with a mass of 30 kDA and it exists only in the extracellular space(8). SOD3 can also be distinguished by its heparin-binding capacity (1).
Superoxide dismutase (SOD) is an endogenously produced intracellular enzyme present in almost every cell in the body (3). It works by catalyzing the dismutation of the superoxide radical O2? to O2 and H2O2, which are then metabolized to H2O and O2 by catalase and glutathione peroxidase (2, 5). In general, SODs play a major role in antioxidant defense mechanisms (4). There are two main types of SOD in mammalian cells. One form (SOD1) contains Cu and Zn ions as a homodimer and exists in the cytoplasm. The two subunits of 16 kDa each are linked by two cysteines forming an intra-subunit disulphide bridge (3). The second form (SOD2) is a manganese containing enzyme and resides in the mitochondrial matrix. It is a homotetramer of 80 kDa. The third form (SOD3 or EC-SOD) is like SOD1 in that it contains Cu and Zn ions, however it is distinct in that it is a homotetramer, with a mass of 30 kDA and it exists only in the extracellular space(8). SOD3 can also be distinguished by its heparin-binding capacity (1).
Aha1 is a member of the HSP90 cochaperone family, and is thought to stimulate HSP90 ATPase activity by competing with p23 and other co-chaperones for HSP90 binding (1, 2). It may affect a step in the endoplasmic reticulum to Golgi trafficking. Aha1 also interacts with HSPCA/HSP90 and with the cytoplasmic tail of the vesicular stomatistis virus glycoproteins (VSV G) (3). Aha1 is expressed in numerous tissues, including the brain, heart, skeletal muscle, and kidney, and at low levels, the liver and placenta. Aha1 might be a potential therapeutic strategy to increase sensitivity to HSP inhibitors (4).
Product Type:
Protein
Format:
20mM HEPES buffer pH7.2, 80mM NaCl, 10% glycerol
Storage Temp:
-20ºC
Applications:
WB | SDS-PAGE | Functional Assay
Target:
AHA1
Conjugate:
No tag
Research Area(s):
Cancer | Heat Shock | Cell Signaling | Protein Trafficking | Chaperone Proteins
Alternative Name(s):
Aha1 Protein, SHSA1 Protein, HSPC322 Protein, p38 Protein
Category:
Recombinant
Accession Number:
NM_036243.1
Gene ID:
10598
Swiss-Prot:
O95433
Purification:
Multi-Step Purified
Concentration:
Lot/batch specific. See included datasheet.
Specificity:
~38 kDa
Certificate of Analysis:
This product has been certified >90% pure using SDS PAGE analysis. 2uM SPR-300 generated a 9-fold ATPase activation of 2uM HSP90 (His-tagged HSP90 beta) in 33mM Hepes pH7.2, 30mM NaCl, 5mM MgCl2, 1mM DTT, 1.5mM ATP in a 100ul reaction at 37 degrees C. (This is an enzyme-linked ATP regeneration assay tracking loss of NADH absorbance at 340nm.)
Cellular Localization:
Cytoplasm
References:
1. Hainzl O., Lapina M.C., Buchner J., Richter K. (2009) J Biol Chem. Epub. 2. Harst A., Lin H., Obermann W.M. (2005) Biochem J. 387 (pt.3): 789-796. 3. Lotz G.P., Brychzy A., Heinz S., Obermann W.M. (2008) J Cell Sci. 121(pt.5): 717-723. 4. Holmes J.L., Sharp S.Y., Hobbs S., Workman P. (2008) Cancer Res. 68(4): 1188-1197.
Aha1 is a member of the HSP90 cochaperone family, and is thought to stimulate HSP90 ATPase activity by competing with p23 and other co-chaperones for HSP90 binding (1, 2). It may affect a step in the endoplasmic reticulum to Golgi trafficking. Aha1 also interacts with HSPCA/HSP90 and with the cytoplasmic tail of the vesicular stomatistis virus glycoproteins (VSV G) (3). Aha1 is expressed in numerous tissues, including the brain, heart, skeletal muscle, and kidney, and at low levels, the liver and placenta. Aha1 might be a potential therapeutic strategy to increase sensitivity to HSP inhibitors (4).
Product Type:
Protein
Format:
20mM HEPES buffer pH7.2, 80mM NaCl, 10% glycerol
Storage Temp:
-20ºC
Applications:
WB | SDS-PAGE | Functional Assay
Target:
AHA1
Conjugate:
No tag
Research Area(s):
Cancer | Heat Shock | Cell Signaling | Protein Trafficking | Chaperone Proteins
Alternative Name(s):
Aha1 Protein, SHSA1 Protein, HSPC322 Protein, p38 Protein
Category:
Recombinant
Accession Number:
NM_036243.1
Gene ID:
10598
Swiss-Prot:
O95433
Purification:
Multi-Step Purified
Concentration:
Lot/batch specific. See included datasheet.
Specificity:
~38 kDa
Certificate of Analysis:
This product has been certified >90% pure using SDS PAGE analysis. 2uM SPR-300 generated a 9-fold ATPase activation of 2uM HSP90 (His-tagged HSP90 beta) in 33mM Hepes pH7.2, 30mM NaCl, 5mM MgCl2, 1mM DTT, 1.5mM ATP in a 100ul reaction at 37 degrees C. (This is an enzyme-linked ATP regeneration assay tracking loss of NADH absorbance at 340nm.)
Cellular Localization:
Cytoplasm
References:
1. Hainzl O., Lapina M.C., Buchner J., Richter K. (2009) J Biol Chem. Epub. 2. Harst A., Lin H., Obermann W.M. (2005) Biochem J. 387 (pt.3): 789-796. 3. Lotz G.P., Brychzy A., Heinz S., Obermann W.M. (2008) J Cell Sci. 121(pt.5): 717-723. 4. Holmes J.L., Sharp S.Y., Hobbs S., Workman P. (2008) Cancer Res. 68(4): 1188-1197.
Aha1 is a member of the HSP90 cochaperone family, and is thought to stimulate HSP90 ATPase activity by competing with p23 and other co-chaperones for HSP90 binding (1, 2). It may affect a step in the endoplasmic reticulum to Golgi trafficking. Aha1 also interacts with HSPCA/HSP90 and with the cytoplasmic tail of the vesicular stomatistis virus glycoproteins (VSV G) (3). Aha1 is expressed in numerous tissues, including the brain, heart, skeletal muscle, and kidney, and at low levels, the liver and placenta. Aha1 might be a potential therapeutic strategy to increase sensitivity to HSP inhibitors (4).
Product Type:
Protein
Format:
20mM HEPES buffer pH7.2, 80mM NaCl, 10% glycerol
Storage Temp:
-20ºC
Applications:
WB | SDS-PAGE | Functional Assay
Target:
AHA1
Conjugate:
No tag
Research Area(s):
Cancer | Heat Shock | Cell Signaling | Protein Trafficking | Chaperone Proteins
Alternative Name(s):
Aha1 Protein, SHSA1 Protein, HSPC322 Protein, p38 Protein
Category:
Recombinant
Accession Number:
NM_036243.1
Gene ID:
10598
Swiss-Prot:
O95433
Purification:
Multi-Step Purified
Concentration:
Lot/batch specific. See included datasheet.
Specificity:
~38 kDa
Certificate of Analysis:
This product has been certified >90% pure using SDS PAGE analysis. 2uM SPR-300 generated a 9-fold ATPase activation of 2uM HSP90 (His-tagged HSP90 beta) in 33mM Hepes pH7.2, 30mM NaCl, 5mM MgCl2, 1mM DTT, 1.5mM ATP in a 100ul reaction at 37 degrees C. (This is an enzyme-linked ATP regeneration assay tracking loss of NADH absorbance at 340nm.)
Cellular Localization:
Cytoplasm
References:
1. Hainzl O., Lapina M.C., Buchner J., Richter K. (2009) J Biol Chem. Epub. 2. Harst A., Lin H., Obermann W.M. (2005) Biochem J. 387 (pt.3): 789-796. 3. Lotz G.P., Brychzy A., Heinz S., Obermann W.M. (2008) J Cell Sci. 121(pt.5): 717-723. 4. Holmes J.L., Sharp S.Y., Hobbs S., Workman P. (2008) Cancer Res. 68(4): 1188-1197.
Hop (HSP70/HSP90 Organizing Protein), or Stress-induced Phosphoprotein 1 (STI1) as it is also known, is a 60kDa protein that belongs to the large group of co-chaperones which regulate and assist the major chaperones. It is located in diverse cellular regions and can move between the cytoplasm and the nucleus. It functions to reversibly link together the protein chaperones HSP70 and HSP90. HOP contains three tetratricopeptide repeat (TPR) domains, TPR1, TPR2a and TPR2b. HSP70 binding has been localized to TRP1 and sp90 binding have been localized to TPR2a (1). It has also been found to modulate the chaperone activities of the linked proteins and possible interacts with other chaperones and proteins. It has also been found to participate in other complexes besides the HSP70/HSP90 one (2). HOP is closely related to human 63kDa protein that is sensitive to simian virus SV40 transformation, and is related to the yeast heat-shock- responsive STI1 gene product (3, 4).
Product Type:
Protein
Format:
20mM HEPES buffer pH7.2, 80mM NaCl, 10% glycerol
Storage Temp:
-20ºC
Applications:
WB | SDS-PAGE | Functional Assay
Target:
HOP
Conjugate:
His tag
Research Area(s):
Cancer | Heat Shock
Alternative Name(s):
HSP co chaperone Protein
Category:
Recombinant
Accession Number:
NP_006810.1
Gene ID:
10963
Swiss-Prot:
P31948
Purification:
Affinity Purified
Concentration:
Lot/batch specific. See included datasheet.
Specificity:
~63 kDa
Certificate of Analysis:
This product has been certified >90% pure using SDS PAGE analysis. 4uM SPR-302, when added to 2uM SPR-300 (Aha1)-activated HSP90 (2uM; His-tagged HSP90 beta) in 33mM Hepes pH7.2, 30mM NaCl, 5mM MgCl2, 1mM DTT, 1.5mM ATP in a 100ul reaction at 37 degrees C, eliminated all Aha1-mediated ATPase stimulation as well as intrinsic HSP90 ATPase activity. (This is an enzyme-linked ATP regeneration assay tracking loss of NADH absorbance at 340nm).
Cellular Localization:
Cytoplasm | Nucleus
References:
1. Flom G., Behal R.H., Rosen L., Cole D.G., Johnson J.L. (2007) Biochem J. 404(1): 159-167. 2. Harst A., Lin H., Obermann W.M. (2005) Biochem J. 387 (pt3): 789-796. 3. Honore B.H., et al. (1992) J Biol Chem. 267: 8485-8491. 4. Nicolet C.M., et al. (1989) Mol Cell Bio. 9: 3638-3646.
Hop (HSP70/HSP90 Organizing Protein), or Stress-induced Phosphoprotein 1 (STI1) as it is also known, is a 60kDa protein that belongs to the large group of co-chaperones which regulate and assist the major chaperones. It is located in diverse cellular regions and can move between the cytoplasm and the nucleus. It functions to reversibly link together the protein chaperones HSP70 and HSP90. HOP contains three tetratricopeptide repeat (TPR) domains, TPR1, TPR2a and TPR2b. HSP70 binding has been localized to TRP1 and sp90 binding have been localized to TPR2a (1). It has also been found to modulate the chaperone activities of the linked proteins and possible interacts with other chaperones and proteins. It has also been found to participate in other complexes besides the HSP70/HSP90 one (2). HOP is closely related to human 63kDa protein that is sensitive to simian virus SV40 transformation, and is related to the yeast heat-shock- responsive STI1 gene product (3, 4).
Product Type:
Protein
Format:
20mM HEPES buffer pH7.2, 80mM NaCl, 10% glycerol
Storage Temp:
-20ºC
Applications:
WB | SDS-PAGE | Functional Assay
Target:
HOP
Conjugate:
His tag
Research Area(s):
Cancer | Heat Shock
Alternative Name(s):
HSP co chaperone Protein
Category:
Recombinant
Accession Number:
NP_006810.1
Gene ID:
10963
Swiss-Prot:
P31948
Purification:
Affinity Purified
Concentration:
Lot/batch specific. See included datasheet.
Specificity:
~63 kDa
Certificate of Analysis:
This product has been certified >90% pure using SDS PAGE analysis. 4uM SPR-302, when added to 2uM SPR-300 (Aha1)-activated HSP90 (2uM; His-tagged HSP90 beta) in 33mM Hepes pH7.2, 30mM NaCl, 5mM MgCl2, 1mM DTT, 1.5mM ATP in a 100ul reaction at 37 degrees C, eliminated all Aha1-mediated ATPase stimulation as well as intrinsic HSP90 ATPase activity. (This is an enzyme-linked ATP regeneration assay tracking loss of NADH absorbance at 340nm).
Cellular Localization:
Cytoplasm | Nucleus
References:
1. Flom G., Behal R.H., Rosen L., Cole D.G., Johnson J.L. (2007) Biochem J. 404(1): 159-167. 2. Harst A., Lin H., Obermann W.M. (2005) Biochem J. 387 (pt3): 789-796. 3. Honore B.H., et al. (1992) J Biol Chem. 267: 8485-8491. 4. Nicolet C.M., et al. (1989) Mol Cell Bio. 9: 3638-3646.
Hop (HSP70/HSP90 Organizing Protein), or Stress-induced Phosphoprotein 1 (STI1) as it is also known, is a 60kDa protein that belongs to the large group of co-chaperones which regulate and assist the major chaperones. It is located in diverse cellular regions and can move between the cytoplasm and the nucleus. It functions to reversibly link together the protein chaperones HSP70 and HSP90. HOP contains three tetratricopeptide repeat (TPR) domains, TPR1, TPR2a and TPR2b. HSP70 binding has been localized to TRP1 and sp90 binding have been localized to TPR2a (1). It has also been found to modulate the chaperone activities of the linked proteins and possible interacts with other chaperones and proteins. It has also been found to participate in other complexes besides the HSP70/HSP90 one (2). HOP is closely related to human 63kDa protein that is sensitive to simian virus SV40 transformation, and is related to the yeast heat-shock- responsive STI1 gene product (3, 4).
Product Type:
Protein
Format:
20mM HEPES buffer pH7.2, 80mM NaCl, 10% glycerol
Storage Temp:
-20ºC
Applications:
WB | SDS-PAGE | Functional Assay
Target:
HOP
Conjugate:
His tag
Research Area(s):
Cancer | Heat Shock
Alternative Name(s):
HSP co chaperone Protein
Category:
Recombinant
Accession Number:
NP_006810.1
Gene ID:
10963
Swiss-Prot:
P31948
Purification:
Affinity Purified
Concentration:
Lot/batch specific. See included datasheet.
Specificity:
~63 kDa
Certificate of Analysis:
This product has been certified >90% pure using SDS PAGE analysis. 4uM SPR-302, when added to 2uM SPR-300 (Aha1)-activated HSP90 (2uM; His-tagged HSP90 beta) in 33mM Hepes pH7.2, 30mM NaCl, 5mM MgCl2, 1mM DTT, 1.5mM ATP in a 100ul reaction at 37 degrees C, eliminated all Aha1-mediated ATPase stimulation as well as intrinsic HSP90 ATPase activity. (This is an enzyme-linked ATP regeneration assay tracking loss of NADH absorbance at 340nm).
Cellular Localization:
Cytoplasm | Nucleus
References:
1. Flom G., Behal R.H., Rosen L., Cole D.G., Johnson J.L. (2007) Biochem J. 404(1): 159-167. 2. Harst A., Lin H., Obermann W.M. (2005) Biochem J. 387 (pt3): 789-796. 3. Honore B.H., et al. (1992) J Biol Chem. 267: 8485-8491. 4. Nicolet C.M., et al. (1989) Mol Cell Bio. 9: 3638-3646.
p23 is a highly conserved ubiquitous protein, known to have an important function as a cochaperone for the HSP90 chaperoning system (1). Studies have revealed that p23 is a small protein (18 to 25 kDa) with a simple structure (2, 3). p23 does not have any structural homology with any other known proteins (1). p23 was first discovered as a part of the HSP90-progesterone receptor complex along with HSP70, p54 and p50 (1). p23 is a phosphor-protein, which is highly acidic and has an aspartic acid-rich c-terminal domain (1). Numerous studies have found p23 to be associated with other client proteins like Fes tyrosine kinase (4), the heme regulated kinase HRI (5), hsf1 transcription factor (4), aryl hydrocarbon receptor (4), telomerase (6), and Hepadnavirus reverse transcriptase (7). In spite of several years of study, the exact functional significance of p23 is still not clear (8). p23 is thought to be involved in the adenosine triphosphatemediated HSP90 binding of client proteins (8). Since many HSP90 client proteins are involved in oncogenic survival signaling, a recent study has concluded p23 to be a promising target in leukemic apoptosis (9). HSP90 and its co-chaperone p23 are certainly among the emerging anti-tumor targets in oncology.
Product Type:
Protein
Format:
20mM HEPES buffer pH7.2, 80mM NaCl, 10% glycerol
Storage Temp:
-20ºC
Applications:
WB | SDS-PAGE | Functional Assay
Target:
p23
Conjugate:
No tag
Research Area(s):
Cancer | Heat Shock
Alternative Name(s):
Sid 3177 Protein, Co chaperone p23 Protein, cPGES Protein, HSP90 co chaperone Protein, cytosolic prostaglandin E2 synthase Protein, PTGES3 Protein, TEBP Protein
Category:
Recombinant
Accession Number:
NP_006592.3
Gene ID:
10728
Swiss-Prot:
Q15185
Purification:
Affinity Purified
Concentration:
Lot/batch specific. See included datasheet.
Specificity:
~23 kDa
Certificate of Analysis:
This product has been certified >90% pure using SDS PAGE analysis. 4uM SPR-303, when added to 2uM SPR-300 (Aha1)-activated HSP90 (2uM; His-tagged HSP90 beta) in 33mM Hepes pH7.2, 30mM NaCl, 5mM MgCl2, 1mM DTT, 1.5mM ATP in a 100ul reaction at 37 degrees C, eliminated all Aha1-mediated ATPase stimulation as well as intrinsic HSP90 ATPase activity. (This is an enzyme-linked ATP regeneration assay tracking loss of NADH absorbance at 340nm).
p23 is a highly conserved ubiquitous protein, known to have an important function as a cochaperone for the HSP90 chaperoning system (1). Studies have revealed that p23 is a small protein (18 to 25 kDa) with a simple structure (2, 3). p23 does not have any structural homology with any other known proteins (1). p23 was first discovered as a part of the HSP90-progesterone receptor complex along with HSP70, p54 and p50 (1). p23 is a phosphor-protein, which is highly acidic and has an aspartic acid-rich c-terminal domain (1). Numerous studies have found p23 to be associated with other client proteins like Fes tyrosine kinase (4), the heme regulated kinase HRI (5), hsf1 transcription factor (4), aryl hydrocarbon receptor (4), telomerase (6), and Hepadnavirus reverse transcriptase (7). In spite of several years of study, the exact functional significance of p23 is still not clear (8). p23 is thought to be involved in the adenosine triphosphatemediated HSP90 binding of client proteins (8). Since many HSP90 client proteins are involved in oncogenic survival signaling, a recent study has concluded p23 to be a promising target in leukemic apoptosis (9). HSP90 and its co-chaperone p23 are certainly among the emerging anti-tumor targets in oncology.
Product Type:
Protein
Format:
20mM HEPES buffer pH7.2, 80mM NaCl, 10% glycerol
Storage Temp:
-20ºC
Applications:
WB | SDS-PAGE | Functional Assay
Target:
p23
Conjugate:
No tag
Research Area(s):
Cancer | Heat Shock
Alternative Name(s):
Sid 3177 Protein, Co chaperone p23 Protein, cPGES Protein, HSP90 co chaperone Protein, cytosolic prostaglandin E2 synthase Protein, PTGES3 Protein, TEBP Protein
Category:
Recombinant
Accession Number:
NP_006592.3
Gene ID:
10728
Swiss-Prot:
Q15185
Purification:
Affinity Purified
Concentration:
Lot/batch specific. See included datasheet.
Specificity:
~23 kDa
Certificate of Analysis:
This product has been certified >90% pure using SDS PAGE analysis. 4uM SPR-303, when added to 2uM SPR-300 (Aha1)-activated HSP90 (2uM; His-tagged HSP90 beta) in 33mM Hepes pH7.2, 30mM NaCl, 5mM MgCl2, 1mM DTT, 1.5mM ATP in a 100ul reaction at 37 degrees C, eliminated all Aha1-mediated ATPase stimulation as well as intrinsic HSP90 ATPase activity. (This is an enzyme-linked ATP regeneration assay tracking loss of NADH absorbance at 340nm).
p23 is a highly conserved ubiquitous protein, known to have an important function as a cochaperone for the HSP90 chaperoning system (1). Studies have revealed that p23 is a small protein (18 to 25 kDa) with a simple structure (2, 3). p23 does not have any structural homology with any other known proteins (1). p23 was first discovered as a part of the HSP90-progesterone receptor complex along with HSP70, p54 and p50 (1). p23 is a phosphor-protein, which is highly acidic and has an aspartic acid-rich c-terminal domain (1). Numerous studies have found p23 to be associated with other client proteins like Fes tyrosine kinase (4), the heme regulated kinase HRI (5), hsf1 transcription factor (4), aryl hydrocarbon receptor (4), telomerase (6), and Hepadnavirus reverse transcriptase (7). In spite of several years of study, the exact functional significance of p23 is still not clear (8). p23 is thought to be involved in the adenosine triphosphatemediated HSP90 binding of client proteins (8). Since many HSP90 client proteins are involved in oncogenic survival signaling, a recent study has concluded p23 to be a promising target in leukemic apoptosis (9). HSP90 and its co-chaperone p23 are certainly among the emerging anti-tumor targets in oncology.
Product Type:
Protein
Format:
20mM HEPES buffer pH7.2, 80mM NaCl, 10% glycerol
Storage Temp:
-20ºC
Applications:
WB | SDS-PAGE | Functional Assay
Target:
p23
Conjugate:
No tag
Research Area(s):
Cancer | Heat Shock
Alternative Name(s):
Sid 3177 Protein, Co chaperone p23 Protein, cPGES Protein, HSP90 co chaperone Protein, cytosolic prostaglandin E2 synthase Protein, PTGES3 Protein, TEBP Protein
Category:
Recombinant
Accession Number:
NP_006592.3
Gene ID:
10728
Swiss-Prot:
Q15185
Purification:
Affinity Purified
Concentration:
Lot/batch specific. See included datasheet.
Specificity:
~23 kDa
Certificate of Analysis:
This product has been certified >90% pure using SDS PAGE analysis. 4uM SPR-303, when added to 2uM SPR-300 (Aha1)-activated HSP90 (2uM; His-tagged HSP90 beta) in 33mM Hepes pH7.2, 30mM NaCl, 5mM MgCl2, 1mM DTT, 1.5mM ATP in a 100ul reaction at 37 degrees C, eliminated all Aha1-mediated ATPase stimulation as well as intrinsic HSP90 ATPase activity. (This is an enzyme-linked ATP regeneration assay tracking loss of NADH absorbance at 340nm).
HSP90 co-chaperone Cdc37 is a protein that is encoded by the CDC37 gene. It has been found to form complexes with HSP90 and a variety of protein kinases including CDK4, CDK6, SRC, RAF1, MOK and elF-2 alpha kinases. It is thought to play a critical role in directing HSP90 to its target kinases (1, 2). CDC37 is necessary for maintaining prostate tumor cell growth and represents a novel target in the exploration for multi-targeted therapies (3, 4).
Product Type:
Protein
Format:
25mM Tris buffer pH7.2, 150mM NaCl, 0.1DTT, 50% glycerol
Storage Temp:
-20ºC
Applications:
WB | SDS-PAGE | Functional Assay
Target:
CDC37
Conjugate:
His tag
Research Area(s):
Cancer | Heat Shock | Cell Signaling | Epigenetics and Nuclear Signaling
Category:
Recombinant
Accession Number:
NP_008996.1
Gene ID:
11140
Swiss-Prot:
Q16543
Purification:
Affinity Purified
Concentration:
Lot/batch specific. See included datasheet.
Specificity:
~445 kDa
Certificate of Analysis:
This product has been certified >90% pure using SDS PAGE analysis. 4uM SPR-303, when added to 2uM SPR-300 (Aha1)-activated HSP90 (2uM; His-tagged HSP90 beta) in 33mM Hepes pH7.2, 30mM NaCl, 5mM MgCl2, 1mM DTT, 1.5mM ATP in a 100ul reaction at 37 degrees C, eliminated all Aha1-mediated ATPase stimulation as well as intrinsic HSP90 ATPase activity. (This is an enzyme-linked ATP regeneration assay tracking loss of NADH absorbance at 340nm).
Cellular Localization:
Cytoplasm
References:
1. Dai K., Kobayashi R., Beach D. (1996) J Biol Chem. 271(36): 22030-22034. 2. Stepanova L., Leng X., Parker S.B., Harper J.W. (1996) Genes Dev. 10(12): 1491-1502. 3. Kimura Y., et al. (1997) Genes Dev. 11(14): 1775-1185. 4. Gray P.J., et al. (2008) Nat Rev Cancer. 8(7): 491-495.
HSP90 co-chaperone Cdc37 is a protein that is encoded by the CDC37 gene. It has been found to form complexes with HSP90 and a variety of protein kinases including CDK4, CDK6, SRC, RAF1, MOK and elF-2 alpha kinases. It is thought to play a critical role in directing HSP90 to its target kinases (1, 2). CDC37 is necessary for maintaining prostate tumor cell growth and represents a novel target in the exploration for multi-targeted therapies (3, 4).
Product Type:
Protein
Format:
25mM Tris buffer pH7.2, 150mM NaCl, 0.1DTT, 50% glycerol
Storage Temp:
-20ºC
Applications:
WB | SDS-PAGE | Functional Assay
Target:
CDC37
Conjugate:
His tag
Research Area(s):
Cancer | Heat Shock | Cell Signaling | Epigenetics and Nuclear Signaling
Category:
Recombinant
Accession Number:
NP_008996.1
Gene ID:
11140
Swiss-Prot:
Q16543
Purification:
Affinity Purified
Concentration:
Lot/batch specific. See included datasheet.
Specificity:
~445 kDa
Certificate of Analysis:
This product has been certified >90% pure using SDS PAGE analysis. 4uM SPR-303, when added to 2uM SPR-300 (Aha1)-activated HSP90 (2uM; His-tagged HSP90 beta) in 33mM Hepes pH7.2, 30mM NaCl, 5mM MgCl2, 1mM DTT, 1.5mM ATP in a 100ul reaction at 37 degrees C, eliminated all Aha1-mediated ATPase stimulation as well as intrinsic HSP90 ATPase activity. (This is an enzyme-linked ATP regeneration assay tracking loss of NADH absorbance at 340nm).
Cellular Localization:
Cytoplasm
References:
1. Dai K., Kobayashi R., Beach D. (1996) J Biol Chem. 271(36): 22030-22034. 2. Stepanova L., Leng X., Parker S.B., Harper J.W. (1996) Genes Dev. 10(12): 1491-1502. 3. Kimura Y., et al. (1997) Genes Dev. 11(14): 1775-1185. 4. Gray P.J., et al. (2008) Nat Rev Cancer. 8(7): 491-495.
HSP90 co-chaperone Cdc37 is a protein that is encoded by the CDC37 gene. It has been found to form complexes with HSP90 and a variety of protein kinases including CDK4, CDK6, SRC, RAF1, MOK and elF-2 alpha kinases. It is thought to play a critical role in directing HSP90 to its target kinases (1, 2). CDC37 is necessary for maintaining prostate tumor cell growth and represents a novel target in the exploration for multi-targeted therapies (3, 4).
Product Type:
Protein
Format:
25mM Tris buffer pH7.2, 150mM NaCl, 0.1DTT, 50% glycerol
Storage Temp:
-20ºC
Applications:
WB | SDS-PAGE | Functional Assay
Target:
CDC37
Conjugate:
His tag
Research Area(s):
Cancer | Heat Shock | Cell Signaling | Epigenetics and Nuclear Signaling
Category:
Recombinant
Accession Number:
NP_008996.1
Gene ID:
11140
Swiss-Prot:
Q16543
Purification:
Affinity Purified
Concentration:
Lot/batch specific. See included datasheet.
Specificity:
~445 kDa
Certificate of Analysis:
This product has been certified >90% pure using SDS PAGE analysis. 4uM SPR-303, when added to 2uM SPR-300 (Aha1)-activated HSP90 (2uM; His-tagged HSP90 beta) in 33mM Hepes pH7.2, 30mM NaCl, 5mM MgCl2, 1mM DTT, 1.5mM ATP in a 100ul reaction at 37 degrees C, eliminated all Aha1-mediated ATPase stimulation as well as intrinsic HSP90 ATPase activity. (This is an enzyme-linked ATP regeneration assay tracking loss of NADH absorbance at 340nm).
Cellular Localization:
Cytoplasm
References:
1. Dai K., Kobayashi R., Beach D. (1996) J Biol Chem. 271(36): 22030-22034. 2. Stepanova L., Leng X., Parker S.B., Harper J.W. (1996) Genes Dev. 10(12): 1491-1502. 3. Kimura Y., et al. (1997) Genes Dev. 11(14): 1775-1185. 4. Gray P.J., et al. (2008) Nat Rev Cancer. 8(7): 491-495.
Aha1 is a member of the HSP90 cochaperone family, and is thought to stimulate HSP90 ATPase activity by competing with p23 and other co-chaperones for HSP90 binding (1, 2). It may affect a step in the endoplasmic reticulum to Golgi trafficking. Aha1 also interacts with HSPCA/HSP90 and with the cytoplasmic tail of the vesicular stomatistis virus glycoproteins (VSV G) (3). Aha1 is expressed in numerous tissues, including the brain, heart, skeletal muscle, and kidney, and at low levels, the liver and placenta. Aha1 might be a potential therapeutic strategy to increase sensitivity to HSP inhibitors (4).
Product Type:
Protein
Format:
20mM HEPES buffer pH7.2, 80mM NaCl, 10% glycerol
Storage Temp:
-20ºC
Applications:
WB | SDS-PAGE | Functional Assay
Target:
AHA1
Conjugate:
His tag
Research Area(s):
Cancer | Heat Shock | Cell Signaling | Protein Trafficking | Chaperone Proteins
Alternative Name(s):
Aha1 Protein, SHSA1 Protein, HSPC322 Protein, p38 Protein
Category:
Recombinant
Accession Number:
NP_036243.1
Gene ID:
10598
Swiss-Prot:
O95433
Purification:
Affinity Purified
Concentration:
Lot/batch specific. See included datasheet.
Specificity:
~38 kDa
Certificate of Analysis:
This product has been certified >90% pure using SDS PAGE analysis. 2uM SPR-309 generated a 9-fold ATPase activation of 2uM HSP90 (His-tagged HSP90 beta) in 33mM Hepes pH7.2, 30mM NaCl, 5mM MgCl2, 1mM DTT, 1.5mM ATP in a 100ul reaction at 37 degrees C. (This is an enzyme-linked ATP regeneration assay tracking loss of NADH absorbance at 340nm.)
Cellular Localization:
Cytoplasm
References:
1. Hainzl O., Lapina M.C., Buchner J., Richter K. (2009) J Biol Chem. Epub. 2. Harst A., Lin H., Obermann W.M. (2005) Biochem J. 387 (pt.3): 789-796. 3. Lotz G.P., Brychzy A., Heinz S., Obermann W.M. (2008) J Cell Sci. 121(pt.5): 717-723. 4. Holmes J.L., Sharp S.Y., Hobbs S., Workman P. (2008) Cancer Res. 68(4): 1188-1197.
Aha1 is a member of the HSP90 cochaperone family, and is thought to stimulate HSP90 ATPase activity by competing with p23 and other co-chaperones for HSP90 binding (1, 2). It may affect a step in the endoplasmic reticulum to Golgi trafficking. Aha1 also interacts with HSPCA/HSP90 and with the cytoplasmic tail of the vesicular stomatistis virus glycoproteins (VSV G) (3). Aha1 is expressed in numerous tissues, including the brain, heart, skeletal muscle, and kidney, and at low levels, the liver and placenta. Aha1 might be a potential therapeutic strategy to increase sensitivity to HSP inhibitors (4).
Product Type:
Protein
Format:
20mM HEPES buffer pH7.2, 80mM NaCl, 10% glycerol
Storage Temp:
-20ºC
Applications:
WB | SDS-PAGE | Functional Assay
Target:
AHA1
Conjugate:
His tag
Research Area(s):
Cancer | Heat Shock | Cell Signaling | Protein Trafficking | Chaperone Proteins
Alternative Name(s):
Aha1 Protein, SHSA1 Protein, HSPC322 Protein, p38 Protein
Category:
Recombinant
Accession Number:
NP_036243.1
Gene ID:
10598
Swiss-Prot:
O95433
Purification:
Affinity Purified
Concentration:
Lot/batch specific. See included datasheet.
Specificity:
~38 kDa
Certificate of Analysis:
This product has been certified >90% pure using SDS PAGE analysis. 2uM SPR-309 generated a 9-fold ATPase activation of 2uM HSP90 (His-tagged HSP90 beta) in 33mM Hepes pH7.2, 30mM NaCl, 5mM MgCl2, 1mM DTT, 1.5mM ATP in a 100ul reaction at 37 degrees C. (This is an enzyme-linked ATP regeneration assay tracking loss of NADH absorbance at 340nm.)
Cellular Localization:
Cytoplasm
References:
1. Hainzl O., Lapina M.C., Buchner J., Richter K. (2009) J Biol Chem. Epub. 2. Harst A., Lin H., Obermann W.M. (2005) Biochem J. 387 (pt.3): 789-796. 3. Lotz G.P., Brychzy A., Heinz S., Obermann W.M. (2008) J Cell Sci. 121(pt.5): 717-723. 4. Holmes J.L., Sharp S.Y., Hobbs S., Workman P. (2008) Cancer Res. 68(4): 1188-1197.
Aha1 is a member of the HSP90 cochaperone family, and is thought to stimulate HSP90 ATPase activity by competing with p23 and other co-chaperones for HSP90 binding (1, 2). It may affect a step in the endoplasmic reticulum to Golgi trafficking. Aha1 also interacts with HSPCA/HSP90 and with the cytoplasmic tail of the vesicular stomatistis virus glycoproteins (VSV G) (3). Aha1 is expressed in numerous tissues, including the brain, heart, skeletal muscle, and kidney, and at low levels, the liver and placenta. Aha1 might be a potential therapeutic strategy to increase sensitivity to HSP inhibitors (4).
Product Type:
Protein
Format:
20mM HEPES buffer pH7.2, 80mM NaCl, 10% glycerol
Storage Temp:
-20ºC
Applications:
WB | SDS-PAGE | Functional Assay
Target:
AHA1
Conjugate:
His tag
Research Area(s):
Cancer | Heat Shock | Cell Signaling | Protein Trafficking | Chaperone Proteins
Alternative Name(s):
Aha1 Protein, SHSA1 Protein, HSPC322 Protein, p38 Protein
Category:
Recombinant
Accession Number:
NP_036243.1
Gene ID:
10598
Swiss-Prot:
O95433
Purification:
Affinity Purified
Concentration:
Lot/batch specific. See included datasheet.
Specificity:
~38 kDa
Certificate of Analysis:
This product has been certified >90% pure using SDS PAGE analysis. 2uM SPR-309 generated a 9-fold ATPase activation of 2uM HSP90 (His-tagged HSP90 beta) in 33mM Hepes pH7.2, 30mM NaCl, 5mM MgCl2, 1mM DTT, 1.5mM ATP in a 100ul reaction at 37 degrees C. (This is an enzyme-linked ATP regeneration assay tracking loss of NADH absorbance at 340nm.)
Cellular Localization:
Cytoplasm
References:
1. Hainzl O., Lapina M.C., Buchner J., Richter K. (2009) J Biol Chem. Epub. 2. Harst A., Lin H., Obermann W.M. (2005) Biochem J. 387 (pt.3): 789-796. 3. Lotz G.P., Brychzy A., Heinz S., Obermann W.M. (2008) J Cell Sci. 121(pt.5): 717-723. 4. Holmes J.L., Sharp S.Y., Hobbs S., Workman P. (2008) Cancer Res. 68(4): 1188-1197.
Chaperonin 10, otherwise known as Cpn10, (groES in E.coli) make up a family of small heart shock proteins with an approximate molecular mass of 10kDa (HSP10s). Cpn10 acts as a co-chaperone and interacts with the HSP60 family to promote proper folding of polypeptides. Cpn10 and Cpn60 both exhibit sevenfold axis of symmetry and function as a team in the protein folding and assembly process (1). Cpn10 has been located in human platelets, but is also present in human maternal serum (2, 3). It has been reported that human Cpn10 is identical with early pregnancy factor, which is involved in control over cell growth and development. This identification suggest that Cpn10 may act like a hormone in stressful situations such as pregnancy (4).
Product Type:
Protein
Format:
20mM Tris, pH7.5, 0.3M NaCl, 10% glycerol, 1 mM DTT
Chaperonin 10, otherwise known as Cpn10, (groES in E.coli) make up a family of small heart shock proteins with an approximate molecular mass of 10kDa (HSP10s). Cpn10 acts as a co-chaperone and interacts with the HSP60 family to promote proper folding of polypeptides. Cpn10 and Cpn60 both exhibit sevenfold axis of symmetry and function as a team in the protein folding and assembly process (1). Cpn10 has been located in human platelets, but is also present in human maternal serum (2, 3). It has been reported that human Cpn10 is identical with early pregnancy factor, which is involved in control over cell growth and development. This identification suggest that Cpn10 may act like a hormone in stressful situations such as pregnancy (4).
Product Type:
Protein
Format:
20mM Tris, pH7.5, 0.3M NaCl, 10% glycerol, 1 mM DTT
Chaperonin 10, otherwise known as Cpn10, (groES in E.coli) make up a family of small heart shock proteins with an approximate molecular mass of 10kDa (HSP10s). Cpn10 acts as a co-chaperone and interacts with the HSP60 family to promote proper folding of polypeptides. Cpn10 and Cpn60 both exhibit sevenfold axis of symmetry and function as a team in the protein folding and assembly process (1). Cpn10 has been located in human platelets, but is also present in human maternal serum (2, 3). It has been reported that human Cpn10 is identical with early pregnancy factor, which is involved in control over cell growth and development. This identification suggest that Cpn10 may act like a hormone in stressful situations such as pregnancy (4).
Product Type:
Protein
Format:
20mM Tris, pH7.5, 0.3M NaCl, 10% glycerol, 1 mM DTT
Aha1 is a member of the HSP90 cochaperone family, and is thought to stimulate HSP90 ATPase activity by competing with p23 and other co-chaperones for HSP90 binding (1, 2). It may affect a step in the endoplasmic reticulum to Golgi trafficking. Aha1 also interacts with HSPCA/HSP90 and with the cytoplasmic tail of the vesicular stomatistis virus glycoproteins (VSV G) (3). Aha1 is expressed in numerous tissues, including the brain, heart, skeletal muscle, and kidney, and at low levels, the liver and placenta. Aha1 might be a potential therapeutic strategy to increase sensitivity to HSP inhibitors (4).
Product Type:
Protein
Format:
25mM Hepes buffer pH7.2, 100mM KoAc, 50% glycerol
Storage Temp:
-20ºC
Applications:
WB | SDS-PAGE | Functional Assay
Target:
AHA1
Conjugate:
His tag
Research Area(s):
Cancer | Heat Shock | Cell Signaling | Protein Trafficking | Chaperone Proteins
Alternative Name(s):
Aha1 Protein, SHSA1 Protein, HSPC322 Protein, p38 Protein
Category:
Recombinant
Accession Number:
NP_666148.1
Gene ID:
217737
Swiss-Prot:
Q8BK64
Purification:
Affinity Purified
Concentration:
Lot/batch specific. See included datasheet.
Specificity:
~38 kDa
Certificate of Analysis:
This product has been certified >90% pure using SDS-PAGE analysis. 2uM SPR-311 generated a 9-fold ATPase activation of 2uM HSP90 (His-tagged HSP90 beta) in 33mM Hepes pH7.2, 30mM NaCl, 5mM MgCl2, 1mM DTT, 1.5mM ATP in a 100ul reaction at 37 degrees C. (This is an enzyme-linked ATP regeneration assay tracking loss of NADH absorbance at 340nm.)
Cellular Localization:
Cytoplasm
References:
1. Hainzl O., Lapina M.C., Buchner J., Richter K. (2009) J Biol Chem. Epub. 2. Harst A., Lin H., Obermann W.M. (2005) Biochem J. 387 (pt.3): 789-796. 3. Lotz G.P., Brychzy A., Heinz S., Obermann W.M. (2008) J Cell Sci. 121(pt.5): 717-723. 4. Holmes J.L., Sharp S.Y., Hobbs S., Workman P. (2008) Cancer Res. 68(4): 1188-1197.
Aha1 is a member of the HSP90 cochaperone family, and is thought to stimulate HSP90 ATPase activity by competing with p23 and other co-chaperones for HSP90 binding (1, 2). It may affect a step in the endoplasmic reticulum to Golgi trafficking. Aha1 also interacts with HSPCA/HSP90 and with the cytoplasmic tail of the vesicular stomatistis virus glycoproteins (VSV G) (3). Aha1 is expressed in numerous tissues, including the brain, heart, skeletal muscle, and kidney, and at low levels, the liver and placenta. Aha1 might be a potential therapeutic strategy to increase sensitivity to HSP inhibitors (4).
Product Type:
Protein
Format:
25mM Hepes buffer pH7.2, 100mM KoAc, 50% glycerol
Storage Temp:
-20ºC
Applications:
WB | SDS-PAGE | Functional Assay
Target:
AHA1
Conjugate:
His tag
Research Area(s):
Cancer | Heat Shock | Cell Signaling | Protein Trafficking | Chaperone Proteins
Alternative Name(s):
Aha1 Protein, SHSA1 Protein, HSPC322 Protein, p38 Protein
Category:
Recombinant
Accession Number:
NP_666148.1
Gene ID:
217737
Swiss-Prot:
Q8BK64
Purification:
Affinity Purified
Concentration:
Lot/batch specific. See included datasheet.
Specificity:
~38 kDa
Certificate of Analysis:
This product has been certified >90% pure using SDS-PAGE analysis. 2uM SPR-311 generated a 9-fold ATPase activation of 2uM HSP90 (His-tagged HSP90 beta) in 33mM Hepes pH7.2, 30mM NaCl, 5mM MgCl2, 1mM DTT, 1.5mM ATP in a 100ul reaction at 37 degrees C. (This is an enzyme-linked ATP regeneration assay tracking loss of NADH absorbance at 340nm.)
Cellular Localization:
Cytoplasm
References:
1. Hainzl O., Lapina M.C., Buchner J., Richter K. (2009) J Biol Chem. Epub. 2. Harst A., Lin H., Obermann W.M. (2005) Biochem J. 387 (pt.3): 789-796. 3. Lotz G.P., Brychzy A., Heinz S., Obermann W.M. (2008) J Cell Sci. 121(pt.5): 717-723. 4. Holmes J.L., Sharp S.Y., Hobbs S., Workman P. (2008) Cancer Res. 68(4): 1188-1197.
Aha1 is a member of the HSP90 cochaperone family, and is thought to stimulate HSP90 ATPase activity by competing with p23 and other co-chaperones for HSP90 binding (1, 2). It may affect a step in the endoplasmic reticulum to Golgi trafficking. Aha1 also interacts with HSPCA/HSP90 and with the cytoplasmic tail of the vesicular stomatistis virus glycoproteins (VSV G) (3). Aha1 is expressed in numerous tissues, including the brain, heart, skeletal muscle, and kidney, and at low levels, the liver and placenta. Aha1 might be a potential therapeutic strategy to increase sensitivity to HSP inhibitors (4).
Product Type:
Protein
Format:
25mM Hepes buffer pH7.2, 100mM KoAc, 50% glycerol
Storage Temp:
-20ºC
Applications:
WB | SDS-PAGE | Functional Assay
Target:
AHA1
Conjugate:
His tag
Research Area(s):
Cancer | Heat Shock | Cell Signaling | Protein Trafficking | Chaperone Proteins
Alternative Name(s):
Aha1 Protein, SHSA1 Protein, HSPC322 Protein, p38 Protein
Category:
Recombinant
Accession Number:
NP_666148.1
Gene ID:
217737
Swiss-Prot:
Q8BK64
Purification:
Affinity Purified
Concentration:
Lot/batch specific. See included datasheet.
Specificity:
~38 kDa
Certificate of Analysis:
This product has been certified >90% pure using SDS-PAGE analysis. 2uM SPR-311 generated a 9-fold ATPase activation of 2uM HSP90 (His-tagged HSP90 beta) in 33mM Hepes pH7.2, 30mM NaCl, 5mM MgCl2, 1mM DTT, 1.5mM ATP in a 100ul reaction at 37 degrees C. (This is an enzyme-linked ATP regeneration assay tracking loss of NADH absorbance at 340nm.)
Cellular Localization:
Cytoplasm
References:
1. Hainzl O., Lapina M.C., Buchner J., Richter K. (2009) J Biol Chem. Epub. 2. Harst A., Lin H., Obermann W.M. (2005) Biochem J. 387 (pt.3): 789-796. 3. Lotz G.P., Brychzy A., Heinz S., Obermann W.M. (2008) J Cell Sci. 121(pt.5): 717-723. 4. Holmes J.L., Sharp S.Y., Hobbs S., Workman P. (2008) Cancer Res. 68(4): 1188-1197.
Aha2 shares 45% sequence homology with Aha1, however, little is known about the functional protein. Aha1 is a member of the HSP90 cochaperone family, and is thought to stimulate HSP90 ATPase activity by competing with p23 and other co-chaperones for HSP90 binding (1, 2). It may affect a step in the endoplasmic reticulum to Golgi trafficking. Aha1 also interacts with HSPCA/HSP90 and with the cytoplasmic tail of the vesicular stomatistis virus glycoproteins (VSV G) (3). Aha1 is expressed in numerous tissues, including the brain, heart, skeletal muscle, and kidney, and at low levels, the liver and placenta. Aha1 might be a potential therapeutic strategy to increase sensitivity to HSP inhibitors (4).
Product Type:
Protein
Format:
100mM NaH2 pH4.5, 10mM Tris buffer with 8M urea
Storage Temp:
-20ºC
Applications:
WB | SDS-PAGE
Target:
AHA2
Conjugate:
His tag
Research Area(s):
Cancer | Heat Shock
Alternative Name(s):
ATPase hydrogen-exporting ATPase 2 Protein
Category:
Recombinant
Accession Number:
NP_036243.1
Gene ID:
130872
Swiss-Prot:
Q719I0
Purification:
Affinity Purified
Concentration:
Lot/batch specific. See included datasheet.
Specificity:
~38 kDa
Certificate of Analysis:
This product has been certified >90% pure using SDS - PAGE analysis.
References:
1. Hainzl O., Lapina M.C., Buchner J., Richter K. (2009) J Biol Chem. Epub. 2. Harst A., Lin H., Obermann W.M. (2005) Biochem J. 387 (pt.3): 789-796. 3. Lotz G.P., Brychzy A., Heinz S., Obermann W.M. (2008) J Cell Sci. 121(pt.5): 717-723. 4. Holmes J.L., Sharp S.Y., Hobbs S., Workman P. (2008) Cancer Res. 68(4): 1188-1197.
Aha2 shares 45% sequence homology with Aha1, however, little is known about the functional protein. Aha1 is a member of the HSP90 cochaperone family, and is thought to stimulate HSP90 ATPase activity by competing with p23 and other co-chaperones for HSP90 binding (1, 2). It may affect a step in the endoplasmic reticulum to Golgi trafficking. Aha1 also interacts with HSPCA/HSP90 and with the cytoplasmic tail of the vesicular stomatistis virus glycoproteins (VSV G) (3). Aha1 is expressed in numerous tissues, including the brain, heart, skeletal muscle, and kidney, and at low levels, the liver and placenta. Aha1 might be a potential therapeutic strategy to increase sensitivity to HSP inhibitors (4).
Product Type:
Protein
Format:
100mM NaH2 pH4.5, 10mM Tris buffer with 8M urea
Storage Temp:
-20ºC
Applications:
WB | SDS-PAGE
Target:
AHA2
Conjugate:
His tag
Research Area(s):
Cancer | Heat Shock
Alternative Name(s):
ATPase hydrogen-exporting ATPase 2 Protein
Category:
Recombinant
Accession Number:
NP_036243.1
Gene ID:
130872
Swiss-Prot:
Q719I0
Purification:
Affinity Purified
Concentration:
Lot/batch specific. See included datasheet.
Specificity:
~38 kDa
Certificate of Analysis:
This product has been certified >90% pure using SDS - PAGE analysis.
References:
1. Hainzl O., Lapina M.C., Buchner J., Richter K. (2009) J Biol Chem. Epub. 2. Harst A., Lin H., Obermann W.M. (2005) Biochem J. 387 (pt.3): 789-796. 3. Lotz G.P., Brychzy A., Heinz S., Obermann W.M. (2008) J Cell Sci. 121(pt.5): 717-723. 4. Holmes J.L., Sharp S.Y., Hobbs S., Workman P. (2008) Cancer Res. 68(4): 1188-1197.
Aha2 shares 45% sequence homology with Aha1, however, little is known about the functional protein. Aha1 is a member of the HSP90 cochaperone family, and is thought to stimulate HSP90 ATPase activity by competing with p23 and other co-chaperones for HSP90 binding (1, 2). It may affect a step in the endoplasmic reticulum to Golgi trafficking. Aha1 also interacts with HSPCA/HSP90 and with the cytoplasmic tail of the vesicular stomatistis virus glycoproteins (VSV G) (3). Aha1 is expressed in numerous tissues, including the brain, heart, skeletal muscle, and kidney, and at low levels, the liver and placenta. Aha1 might be a potential therapeutic strategy to increase sensitivity to HSP inhibitors (4).
Product Type:
Protein
Format:
100mM NaH2 pH4.5, 10mM Tris buffer with 8M urea
Storage Temp:
-20ºC
Applications:
WB | SDS-PAGE
Target:
AHA2
Conjugate:
His tag
Research Area(s):
Cancer | Heat Shock
Alternative Name(s):
ATPase hydrogen-exporting ATPase 2 Protein
Category:
Recombinant
Accession Number:
NP_036243.1
Gene ID:
130872
Swiss-Prot:
Q719I0
Purification:
Affinity Purified
Concentration:
Lot/batch specific. See included datasheet.
Specificity:
~38 kDa
Certificate of Analysis:
This product has been certified >90% pure using SDS - PAGE analysis.
References:
1. Hainzl O., Lapina M.C., Buchner J., Richter K. (2009) J Biol Chem. Epub. 2. Harst A., Lin H., Obermann W.M. (2005) Biochem J. 387 (pt.3): 789-796. 3. Lotz G.P., Brychzy A., Heinz S., Obermann W.M. (2008) J Cell Sci. 121(pt.5): 717-723. 4. Holmes J.L., Sharp S.Y., Hobbs S., Workman P. (2008) Cancer Res. 68(4): 1188-1197.
Aha2 shares 45% sequence homology with Aha1, however, little is known about the functional protein. Aha1 is a member of the HSP90 cochaperone family, and is thought to stimulate HSP90 ATPase activity by competing with p23 and other co-chaperones for HSP90 binding (1, 2). It may affect a step in the endoplasmic reticulum to Golgi trafficking. Aha1 also interacts with HSPCA/HSP90 and with the cytoplasmic tail of the vesicular stomatistis virus glycoproteins (VSV G) (3). Aha1 is expressed in numerous tissues, including the brain, heart, skeletal muscle, and kidney, and at low levels, the liver and placenta. Aha1 might be a potential therapeutic strategy to increase sensitivity to HSP inhibitors (4).
Aha2 shares 45% sequence homology with Aha1, however, little is known about the functional protein. Aha1 is a member of the HSP90 cochaperone family, and is thought to stimulate HSP90 ATPase activity by competing with p23 and other co-chaperones for HSP90 binding (1, 2). It may affect a step in the endoplasmic reticulum to Golgi trafficking. Aha1 also interacts with HSPCA/HSP90 and with the cytoplasmic tail of the vesicular stomatistis virus glycoproteins (VSV G) (3). Aha1 is expressed in numerous tissues, including the brain, heart, skeletal muscle, and kidney, and at low levels, the liver and placenta. Aha1 might be a potential therapeutic strategy to increase sensitivity to HSP inhibitors (4).
Aha2 shares 45% sequence homology with Aha1, however, little is known about the functional protein. Aha1 is a member of the HSP90 cochaperone family, and is thought to stimulate HSP90 ATPase activity by competing with p23 and other co-chaperones for HSP90 binding (1, 2). It may affect a step in the endoplasmic reticulum to Golgi trafficking. Aha1 also interacts with HSPCA/HSP90 and with the cytoplasmic tail of the vesicular stomatistis virus glycoproteins (VSV G) (3). Aha1 is expressed in numerous tissues, including the brain, heart, skeletal muscle, and kidney, and at low levels, the liver and placenta. Aha1 might be a potential therapeutic strategy to increase sensitivity to HSP inhibitors (4).
Aha1 is a member of the HSP90 cochaperone family, and is thought to stimulate HSP90 ATPase activity by competing with p23 and other co-chaperones for HSP90 binding (1, 2). It may affect a step in the endoplasmic reticulum to Golgi trafficking. Aha1 also interacts with HSPCA/HSP90 and with the cytoplasmic tail of the vesicular stomatistis virus glycoproteins (VSV G) (3). Aha1 is expressed in numerous tissues, including the brain, heart, skeletal muscle, and kidney, and at low levels, the liver and placenta. Aha1 might be a potential therapeutic strategy to increase sensitivity to HSP inhibitors (4).
Aha1 is a member of the HSP90 cochaperone family, and is thought to stimulate HSP90 ATPase activity by competing with p23 and other co-chaperones for HSP90 binding (1, 2). It may affect a step in the endoplasmic reticulum to Golgi trafficking. Aha1 also interacts with HSPCA/HSP90 and with the cytoplasmic tail of the vesicular stomatistis virus glycoproteins (VSV G) (3). Aha1 is expressed in numerous tissues, including the brain, heart, skeletal muscle, and kidney, and at low levels, the liver and placenta. Aha1 might be a potential therapeutic strategy to increase sensitivity to HSP inhibitors (4).
Chaperonin 10, otherwise known as Cpn10, (groES in E.coli) make up a family of small heart shock proteins with an approximate molecular mass of 10kDa (HSP10s). Cpn10 acts as a co-chaperone and interacts with the HSP60 family to promote proper folding of polypeptides. Cpn10 and Cpn60 both exhibit sevenfold axis of symmetry and function as a team in the protein folding and assembly process (1). Cpn10 has been located in human platelets, but is also present in human maternal serum (2, 3). It has been reported that human Cpn10 is identical with early pregnancy factor, which is involved in control over cell growth and development. This identification suggest that Cpn10 may act like a hormone in stressful situations such as pregnancy (4).
Heme-oxygenase is a ubiquitous enzyme that catalyzes the initial and rate-limiting steps in heme catabolism yielding equimolar amounts of biliverdin, iron and carbon monoxide. Biliverdin is subsequently converted to bilirubin and the free iron is sequestered to ferritin (1). These products have important physiological effects as carbon monoxide is a potent vasodilator; biliverdin and bilirubin are potent antioxidants; and the free iron increases oxidative stress and regulates the expression of many mRNAs (2).There are three isoforms of heme-oxygenase, HO-1, HO-2 and HO-3; however HO-1 and HO-2 are the major isoforms as they both have been identified in mammals (3). HO-1, also known as heat shock protein 32, is an inducible isoform activated by most oxidative stress inducers, cytokines, inflammatory agents and heat shock. HO-2 is a constitutive isoform which is expressed under homeostatic conditions. HO-1 is also considered to be a cytoprotective factor in that free heme is highly reactive and cytotoxic, and secondly, carbon monoxide is a mediator inhibiting the inflammatory process and bilirubin is a scavenger for reactive oxygen, both of which are the end products of heme catalyzation (4). It has also been shown that HO-1 deficiency may cause reduced stress defense, a pro-inflammatory tendency (5), susceptibility to atherosclerotic lesion formation (6), endothelial cell injury, and growth retardation (7). Up-regulation of HO-1 is therefore said to be one of the major defense mechanisms of oxidative stress (4).
Heme oxygenase 1 Protein, Hemox Protein, HMOX1 Protein, HO1 Protein, HO 1 Protein, HSP32 Protein
Category:
Recombinant
Accession Number:
NP_036712.1
Gene ID:
24451
Swiss-Prot:
P06762
Purification:
Affinity Purified
Concentration:
Lot/batch specific. See included datasheet.
Specificity:
~32 kDa
Certificate of Analysis:
This product has been certified >90% pure using SDSPAGE analysis.
Cellular Localization:
Microsome | Endoplasmic Reticulum
References:
1. Froh M. et al. (2007) World J. Gastroentereol 13(25): 3478-86. 2. Elbirt K.K. and Bonkovsky H.L. (1999) Proc Assoc Am Physicians 111(5): 348-47. 3. Maines M.D., Trakshel G.M., and Kutty R.K. (1986) J Biol Chem 261: 411419. 4. Brydun A., et al. (2007) Hypertens Res 30(4): 341-8. 5. Poss K.D. and Tonegawa S. (1997). Proc Natl Acad Sci U S A. 94: 1092510930. 6. Yet S.F., et al. (2003) FASEB J. 17: 17591761. 7. Yachie A., et al. (1999) J Clin Invest. 103: 129135.
Heme-oxygenase is a ubiquitous enzyme that catalyzes the initial and rate-limiting steps in heme catabolism yielding equimolar amounts of biliverdin, iron and carbon monoxide. Biliverdin is subsequently converted to bilirubin and the free iron is sequestered to ferritin (1). These products have important physiological effects as carbon monoxide is a potent vasodilator; biliverdin and bilirubin are potent antioxidants; and the free iron increases oxidative stress and regulates the expression of many mRNAs (2).There are three isoforms of heme-oxygenase, HO-1, HO-2 and HO-3; however HO-1 and HO-2 are the major isoforms as they both have been identified in mammals (3). HO-1, also known as heat shock protein 32, is an inducible isoform activated by most oxidative stress inducers, cytokines, inflammatory agents and heat shock. HO-2 is a constitutive isoform which is expressed under homeostatic conditions. HO-1 is also considered to be a cytoprotective factor in that free heme is highly reactive and cytotoxic, and secondly, carbon monoxide is a mediator inhibiting the inflammatory process and bilirubin is a scavenger for reactive oxygen, both of which are the end products of heme catalyzation (4). It has also been shown that HO-1 deficiency may cause reduced stress defense, a pro-inflammatory tendency (5), susceptibility to atherosclerotic lesion formation (6), endothelial cell injury, and growth retardation (7). Up-regulation of HO-1 is therefore said to be one of the major defense mechanisms of oxidative stress (4).
Heme oxygenase 1 Protein, Hemox Protein, HMOX1 Protein, HO1 Protein, HO 1 Protein, HSP32 Protein
Category:
Recombinant
Accession Number:
NP_036712.1
Gene ID:
24451
Swiss-Prot:
P06762
Purification:
Affinity Purified
Concentration:
Lot/batch specific. See included datasheet.
Specificity:
~32 kDa
Certificate of Analysis:
This product has been certified >90% pure using SDSPAGE analysis.
Cellular Localization:
Microsome | Endoplasmic Reticulum
References:
1. Froh M. et al. (2007) World J. Gastroentereol 13(25): 3478-86. 2. Elbirt K.K. and Bonkovsky H.L. (1999) Proc Assoc Am Physicians 111(5): 348-47. 3. Maines M.D., Trakshel G.M., and Kutty R.K. (1986) J Biol Chem 261: 411419. 4. Brydun A., et al. (2007) Hypertens Res 30(4): 341-8. 5. Poss K.D. and Tonegawa S. (1997). Proc Natl Acad Sci U S A. 94: 1092510930. 6. Yet S.F., et al. (2003) FASEB J. 17: 17591761. 7. Yachie A., et al. (1999) J Clin Invest. 103: 129135.
Heme-oxygenase is a ubiquitous enzyme that catalyzes the initial and rate-limiting steps in heme catabolism yielding equimolar amounts of biliverdin, iron and carbon monoxide. Biliverdin is subsequently converted to bilirubin and the free iron is sequestered to ferritin (1). These products have important physiological effects as carbon monoxide is a potent vasodilator; biliverdin and bilirubin are potent antioxidants; and the free iron increases oxidative stress and regulates the expression of many mRNAs (2).There are three isoforms of heme-oxygenase, HO-1, HO-2 and HO-3; however HO-1 and HO-2 are the major isoforms as they both have been identified in mammals (3). HO-1, also known as heat shock protein 32, is an inducible isoform activated by most oxidative stress inducers, cytokines, inflammatory agents and heat shock. HO-2 is a constitutive isoform which is expressed under homeostatic conditions. HO-1 is also considered to be a cytoprotective factor in that free heme is highly reactive and cytotoxic, and secondly, carbon monoxide is a mediator inhibiting the inflammatory process and bilirubin is a scavenger for reactive oxygen, both of which are the end products of heme catalyzation (4). It has also been shown that HO-1 deficiency may cause reduced stress defense, a pro-inflammatory tendency (5), susceptibility to atherosclerotic lesion formation (6), endothelial cell injury, and growth retardation (7). Up-regulation of HO-1 is therefore said to be one of the major defense mechanisms of oxidative stress (4).
Heme oxygenase 1 Protein, Hemox Protein, HMOX1 Protein, HO1 Protein, HO 1 Protein, HSP32 Protein
Category:
Recombinant
Accession Number:
NP_036712.1
Gene ID:
24451
Swiss-Prot:
P06762
Purification:
Affinity Purified
Concentration:
Lot/batch specific. See included datasheet.
Specificity:
~32 kDa
Certificate of Analysis:
This product has been certified >90% pure using SDSPAGE analysis.
Cellular Localization:
Microsome | Endoplasmic Reticulum
References:
1. Froh M. et al. (2007) World J. Gastroentereol 13(25): 3478-86. 2. Elbirt K.K. and Bonkovsky H.L. (1999) Proc Assoc Am Physicians 111(5): 348-47. 3. Maines M.D., Trakshel G.M., and Kutty R.K. (1986) J Biol Chem 261: 411419. 4. Brydun A., et al. (2007) Hypertens Res 30(4): 341-8. 5. Poss K.D. and Tonegawa S. (1997). Proc Natl Acad Sci U S A. 94: 1092510930. 6. Yet S.F., et al. (2003) FASEB J. 17: 17591761. 7. Yachie A., et al. (1999) J Clin Invest. 103: 129135.
Human Recombinant Alpha Synuclein Protein Monomer (Control)
Background Info:
Alpha-Synuclein (SNCA) is expressed predominantly in the brain, where it is concentrated in presynaptic nerve terminals (1). Alpha-synuclein is highly expressed in the mitochondria of the olfactory bulb, hippocampus, striatum and thalamus (2). Functionally, it has been shown to significantly interact with tubulin (3), and may serve as a potential microtubule-associated protein. It has also been found to be essential for normal development of the cognitive functions; inactivation may lead to impaired spatial learning and working memory (4). SNCA fibrillar aggregates represent the major non A-beta component of Alzheimers disease amyloid plaque, and a major component of Lewy body inclusions, and Parkinson's disease. Parkinson's disease (PD) is a common neurodegenerative disorder characterized by the progressive accumulation in selected neurons of protein inclusions containing alpha-synuclein and ubiquitin (5, 6).
Human Recombinant Alpha Synuclein Protein Monomer (Control)
Background Info:
Alpha-Synuclein (SNCA) is expressed predominantly in the brain, where it is concentrated in presynaptic nerve terminals (1). Alpha-synuclein is highly expressed in the mitochondria of the olfactory bulb, hippocampus, striatum and thalamus (2). Functionally, it has been shown to significantly interact with tubulin (3), and may serve as a potential microtubule-associated protein. It has also been found to be essential for normal development of the cognitive functions; inactivation may lead to impaired spatial learning and working memory (4). SNCA fibrillar aggregates represent the major non A-beta component of Alzheimers disease amyloid plaque, and a major component of Lewy body inclusions, and Parkinson's disease. Parkinson's disease (PD) is a common neurodegenerative disorder characterized by the progressive accumulation in selected neurons of protein inclusions containing alpha-synuclein and ubiquitin (5, 6).
Human Recombinant Alpha Synuclein Protein Monomer (Control)
Background Info:
Alpha-Synuclein (SNCA) is expressed predominantly in the brain, where it is concentrated in presynaptic nerve terminals (1). Alpha-synuclein is highly expressed in the mitochondria of the olfactory bulb, hippocampus, striatum and thalamus (2). Functionally, it has been shown to significantly interact with tubulin (3), and may serve as a potential microtubule-associated protein. It has also been found to be essential for normal development of the cognitive functions; inactivation may lead to impaired spatial learning and working memory (4). SNCA fibrillar aggregates represent the major non A-beta component of Alzheimers disease amyloid plaque, and a major component of Lewy body inclusions, and Parkinson's disease. Parkinson's disease (PD) is a common neurodegenerative disorder characterized by the progressive accumulation in selected neurons of protein inclusions containing alpha-synuclein and ubiquitin (5, 6).
Human Recombinant Alpha Synuclein Preformed Fibrils (Control)
Background Info:
Alpha-Synuclein (SNCA) is expressed predominantly in the brain, where it is concentrated in presynaptic nerve terminals (1). Alpha-synuclein is highly expressed in the mitochondria of the olfactory bulb, hippocampus, striatum and thalamus (2). Functionally, it has been shown to significantly interact with tubulin (3), and may serve as a potential microtubule-associated protein. It has also been found to be essential for normal development of the cognitive functions; inactivation may lead to impaired spatial learning and working memory (4). SNCA fibrillar aggregates represent the major non A-beta component of Alzheimers disease amyloid plaque, and a major component of Lewy body inclusions, and Parkinson's disease. Parkinson's disease (PD) is a common neurodegenerative disorder characterized by the progressive accumulation in selected neurons of protein inclusions containing alpha-synuclein and ubiquitin (5, 6).
Alpha synuclein PFFs, Alpha synuclein aggregates, Alpha synuclein protein aggregates, Alpha synuclein aggregates, Alpha-synuclein protein, Non-A beta component of AD amyloid protein, Non-A4 component of amyloid precursor protein, NACP protein, SNCA protein, NACP protein, PARK1 protein, SYN protein, Parkison disease familial 1 Protein
Category:
Recombinant
Accession Number:
NP_000336.1
Gene ID:
6622
Swiss-Prot:
P37840
Purification:
Ion-exchange Purified
Concentration:
Lot/batch specific. See included datasheet.
Specificity:
~14.46 kDa
Certificate of Analysis:
Certified 92% pure using SDS-PAGE analysis.
Cellular Localization:
Cytoplasm | Membrane | Nucleus
References:
1. Genetics Home Reference: SNCA. US National Library of Medicine. (2013). 2. Zhang L., et al. (2008) Brain Res. 1244: 40-52. 3. Alim M.A., et al. (2002) J Biol Chem. 277(3): 2112-2117. 4. Kokhan V.S., Afanasyeva M.A., Van'kin G. (2012) Behav. Brain. Res. 231(1): 226-230. 5. Spillantini M.G., et al. (1997) Nature. 388(6645): 839-840. 6. Mezey E., et al. (1998) Nat Med. 4(7): 755-757.
Tarriff Code:
3822.00.1090
ADR Code:
Non-hazardous
UN Code for transport:
Non-hazardous
Country of Origin:
Canada
Biological Activity:
Does not induce Lewy body inclusion formation in Sprague-Dawley rat primary hippocampal neurons. Thioflavin T emission curve does not show an increase in fluorescence (which would indicate alpha synuclein aggregation) when control alpha synuclein PFFs (SPR-317) are combined with active alpha synuclein monomer (SPR-321) or control alpha synuclein monomer (SPR-316). Certain biological activities in other neuronal cells cannot be ruled out. Researchers should test compatibility prior to use.
Human Recombinant Alpha Synuclein Preformed Fibrils (Control)
Background Info:
Alpha-Synuclein (SNCA) is expressed predominantly in the brain, where it is concentrated in presynaptic nerve terminals (1). Alpha-synuclein is highly expressed in the mitochondria of the olfactory bulb, hippocampus, striatum and thalamus (2). Functionally, it has been shown to significantly interact with tubulin (3), and may serve as a potential microtubule-associated protein. It has also been found to be essential for normal development of the cognitive functions; inactivation may lead to impaired spatial learning and working memory (4). SNCA fibrillar aggregates represent the major non A-beta component of Alzheimers disease amyloid plaque, and a major component of Lewy body inclusions, and Parkinson's disease. Parkinson's disease (PD) is a common neurodegenerative disorder characterized by the progressive accumulation in selected neurons of protein inclusions containing alpha-synuclein and ubiquitin (5, 6).
