Lindhagen-Persson et al. (2010). Amyloid-\x{03b2} oligomer specificity mediated by the IgM isotype--implications for a specific protective mechanism exerted by endogenous auto-antibodies. PLoS One. 2010 Nov 10;5(11):e13928. doi: 10.1371/journal.pone.0013928.
Product Type:
Antibody
Antibody Type:
Polyclonal
Format:
Lyophilized
Storage Temp:
Store lyophilized/reconstituted at -20°C; once reconstituted make aliquots to avoid repeated freeze-thaw cycles. Please, remember to spin tubes briefly prior to opening them to avoid any losses that might occur from lyophilized material adhering to the cap or sides of the tubes.
Host Animal:
Rabbit
Species Reactivity:
Human
Expected Species:
Bovine, Chicken, Dog, Porcine, Rabbit
Immunogen:
synthetic peptide chosen from human Abeta (1-42) protein. Amino acid sequence: D-A-E-F-R-H-D-S-G-Y-E-V-H-H-Q-K-L-V-F-F-A-E-D-V-G-S-N-K-G-A-I-I-G-L-M-V-G-G-V-V-I-A
Applications:
Dot Blot (Dot), ELISA (ELISA), Immunolocalization (IL), Western blot (WB)
The antibody can detect Abeta (1-42), Abeta (1-28) Abeta (1-20) and Abeta (1-17). This product exhibits a low reactivity to monomeric Abeta (1-42) as determined by SDS-PAGE and Western blotting.Immunolocalization: human tissue was paraffin-embedded and sectioned. De-waxed and rehydrated in an ethanol gradient. Antigens were retrieved in sodium citrate buffer (pH 6) at 95°C for 1 h. The tissue sections were separately incubated for 1 h at RT with primary antibody and antibody binding was visualized with IgG Preoxidase Reagent Kit.
Application Details:
1 : 1000 (DB), 1 : 3000 (ELISA), 1-2 µg/ml (IL)
Purity:
Serum
Reconstitution:
For reconstitution add 100 µl of sterile water.
Related products:
Alzheimer | available antibodies for Alzheimer's disease | Amyloid beta research
Molecular Weight:
4.5 kDa
Not reactive in:
No confirmed exceptions from predicted reactivity are currently known.
Selected references:
Lupette et al. (2019). The architecture of lipid droplets in the diatom Phaeodactylum tricornutum. Algal Research Volume 38, March 2019, 101415.Singh et al. (2018). A single class of ARF GTPase activated by several pathway-specific ARF-GEFs regulates essential membrane traffic in Arabidopsis. PLoS Genet. 2018 Nov 15;14(11):e1007795. doi: 10.1371/journal.pgen.1007795.Kitakura et al. (2017). BEN3/BIG2 ARF GEF is Involved in Brefeldin A-Sensitive Trafficking at the trans-Golgi Network/Early Endosome in Arabidopsis thaliana. Plant Cell Physiol. 2017 Oct 1;58(10):1801-1811. doi: 10.1093/pcp/pcx118.Nagel et al. (2017). Arabidopsis SH3P2 is an ubiquitin-binding protein that functions together with ESCRT-I and the deubiquitylating enzyme AMSH3. Proc Natl Acad Sci U S A. 2017 Aug 7. pii: 201710866. doi: 10.1073/pnas.1710866114.Wattelet-Boyer et al. (2016). Enrichment of hydroxylated C24- and C26-acyl- chain sphingolipids mediates PIN2 apical sorting at trans-Golgi network subdomains. Nat Commun. 2016 Sep 29;7:12788. doi: 10.1038/ncomms12788.Derbyshire et al. (2015). Proteomic Analysis of Microtubule Interacting Proteins over the Course of Xylem Tracheary Element Formation in Arabidopsis. Plant Cell. 2015 Oct 2. pii: tpc.15.00314.Tanaka et al. (2013). Cell Polarity and Patterning by PIN Trafficking through Early Endosomal Compartments in Arabidopsis thaliana. PLoS Genet. May;9(5). (immunolocalization).Hopff et al. (2013). The plasma membrane proteome of maize roots grown under low and high iron conditions. J Proteomics Jan 24.Pimpl et al (2000). In situ localization and in vitro induction of plant COPI-coated vesicles. Plant Cell. 2000 Nov;12(11):2219-36.
Special application note:
Alzheimer's disease (AD) is the most prevalent neurodegenerative disease in the growing population of elderly people. A hallmark of AD is the accumulation of plaques in the brain of AD patients. The plaques predominantly consist of aggregates of amyloid-beta (Abeta), a peptide of 39-42 amino acids generated in vivo by specific, proteolytic cleavage of the amyloid precursor protein P05067
Store lyophilized/reconstituted at -20°C; once reconstituted make aliquots to avoid repeated freeze-thaw cycles. Please, remember to spin tubes briefly prior to opening them to avoid any losses that might occur from lyophilized material adhering to the cap or sides of the tubes. Do not Store this antibody in 4°C.
Host Animal:
Chicken
Species Reactivity:
Human
Expected Species:
Bovine, Chicken, Dog, Porcine, Rabbit
Immunogen:
synthetic peptide chosen from human Abeta (1-42) protein. Amino acid sequence: D-A-E-F-R-H-D-S-G-Y-E-V-H-H-Q-K-L-V-F-F-A-E-D-V-G-S-N-K-G-A-I-I-G-L-M-V-G-G-V-V-I-A
The antibody can detect Abeta(1-42), but does not react with Abeta(1-28) Abeta(1-20) or Abeta(1-17).
Application Details:
1 : 1000 (Dot), 1 : 500 (ELISA)
Purity:
Total IgY
Related products:
Alzheimer | available antibodies for Alzheimer's disease | Amyloid beta research
Molecular Weight:
4.5 kDa
Not reactive in:
No confirmed exceptions from predicted reactivity are currently known.
Selected references:
Lindhagen-Persson et al. (2010). Amyloid-\x{03b2} oligomer specificity mediated by the IgM isotype--implications for a specific protective mechanism exerted by endogenous auto-antibodies. PLoS One. 2010 Nov 10;5(11):e13928. doi: 10.1371/journal.pone.0013928.
Special application note:
Alzheimer's disease (AD) is the most prevalent neurodegenerative disease in the growing population of elderly people. A hallmark of AD is the accumulation of plaques in the brain of AD patients. The plaques predominantly consist of aggregates of amyloid-beta (Abeta), a peptide of 39-42 amino acids generated in vivo by specific, proteolytic cleavage of the amyloid precursor protein P05067
Store at 4°C; make aliquots to avoid working with a stock. Please, remember to spin tubes briefly prior to opening them to avoid any losses that might occur from liquid material adhering to the cap or sides of the tubes.
Host Animal:
Rabbit
Species Reactivity:
Human
Expected Species:
Bovine, Chicken, Dog, Porcine, Rabbit
Immunogen:
synthetic peptide chosen from human Abeta (1-42) protein. Amino acid sequence: D-A-E-F-R-H-D-S-G-Y-E-V-H-H-Q-K-L-V-F-F-A-E-D-V-G-S-N-K-G-A-I-I-G-L-M-V-G-G-V-V-I-A
The antibody can detect Abeta(1-42), Abeta(1-28) Abeta(1-20) and Abeta(1-17).
Application Details:
1 : 1000 (Dot), 1 : 3000 (ELISA), 1 : 1000 (WB)
Purity:
Serum
Reconstitution:
For reconstitution add 100 µl of sterile water.
Related products:
Alzheimer | available antibodies for Alzheimer's disease | Amyloid beta research
Molecular Weight:
4.5 kDa
Not reactive in:
No confirmed exceptions from predicted reactivity are currently known.
Special application note:
Alzheimer's disease (AD) is the most prevalent neurodegenerative disease in the growing population of elderly people. A hallmark of AD is the accumulation of plaques in the brain of AD patients. The plaques predominantly consist of aggregates of amyloid-beta (Abeta), a peptide of 39-42 amino acids generated in vivo by specific, proteolytic cleavage of the amyloid precursor protein P05067
Henning-Knechtel et al. (2020). Designed Cell-Penetrating Peptide Inhibitors of Amyloid-beta Aggregation and Cytotoxicity. Cell Reports Physical Science,Volume 1, Issue 2, 26Oh et al. (2020). Associative Interactions among Zinc, Apolipoprotein E, and Amyloid-�² in the Amyloid Pathology. Int J Mol Sci. 2020 Jan 25;21(3). pii: E802. doi: 10.3390/ijms21030802.Zhang et al. (2019). Brains of rhesus monkeys display A\x{03b2} deposits and glial pathology while lacking A\x{03b2} dimers and other Alzheimer's pathologies. Aging Cell. 2019 Jun 4:e12978. doi: 10.1111/acel.12978.Kumar et al. (2018). Peptidomimetic-Based Multidomain Targeting Offers Critical Evaluation of A\x{03b2} Structure and Toxic Function. J Am Chem Soc. 2018 May 30;140(21):6562-6574. doi: 10.1021/jacs.7b13401.Kumar et al. (2017). Foldamer-Mediated Structural Rearrangement Attenuates A\x{03b2} Oligomerization and Cytotoxicity. J Am Chem Soc. 2017 Nov 29;139(47):17098-17108. doi: 10.1021/jacs.7b08259. Zhao et al. (2016). Antiamyloidogenic Activity of A\x{03b2}42-Binding Peptoid in Modulating Amyloid Oligomerization. Small. 2016 Oct 7. doi: 10.1002/smll.201602857.Richman et al. (2013). In Vitro and Mechanistic Studies of an Anti-Amyloidogenic Self-Assembled Cyclic D,L-#-Peptide Architecture. J. Americal Chemical Societ, Jan 19.Lindhagen-Persson et al. (2010). Amyloid-\x{03b2} Oligomer Specificity Mediated by the IgM Isotype \x{2013} Implications for a Specific Protective Mechanism Exerted by Endogenous Auto-Antibodies. PLoS ONE.
Product Type:
Antibody
Antibody Type:
Monoclonal
Format:
Lyophilized
Storage Temp:
Store at 2-8°C. Shelf life is one year from date of receipt.
Host Animal:
Mouse
Species Reactivity:
Human Abeta oligomers only
Expected Species:
Rat
Immunogen:
partly aggregated, recombinant peptide corresponding to the human Abeta (1-40/42). Amino acid sequence: D-A-E-F-R-H-D-S-G-Y-E-V-H-H-Q-K-L-V-F-F-A-E-D-V-G-S-N-K-G-A-I-I-G-L-M-V-G-G-V-V. The epitope is 3-8. Molecular weight of immunogen is 4.5 kDa.
OMAB antibody is a versatile tool within research of Alzheimer\x{2019}s disease. A sandwhich ELISA illustrates its potential regarding its high selectivity towards A\x{03b2} oligomers.
Clone number:
IgM
Application Details:
Coating antibody at 2 µg/ml (ELISA), 1 : 500 (IHC)
Purity:
Affinity purified
Reconstitution:
For reconstitution add 100 µl of sterile water.
Related products:
AS13 2716 | mAB-M | human Abeta protein (3-10) region, oligomer-specific, mouse monoclonal antibodyAS13 2715 | mAB-O | human Abeta protein (3-10) region, oligomer specific, mouse monoclonal antibodyAS10 932B | Amyloid beta oligomer-specific monoclonal antibody (OMAB), BiotinylatedAgrisera matching secondary antibody: Goat anti-mouse IgM (µ chain), HRP conjugated, min. cross-reactivity to human IgG/serum, AS10 969Secondary antibodies | Amyloid beta research
Molecular Weight:
4.5 kDa
Not reactive in:
No confirmed exceptions from predicted reactivity are currently known.
Selected references:
to be added when available
Special application note:
Soluble oligomeric assemblies of the Amyloid-\x{03b2} peptide are today anticipated to be the direct cause regarding the Alzheimer pathology. As a consequence, oligomeric A\x{03b2}-assemblies constitute a very interesting therapeutic target. Identification of A\x{03b2}-oligomers is however, technically challenging due to there labile nature and low abundance. Abeta oligomer-specific OMAB antibody is based on the IgM isotype and represents a new concept of A\x{03b2}-oligomer binders using a combination of high avidity and very low monovalent affinity. This combination creates a selectivity of the antibody towards the oligomeric fraction and minimizes reactivity towards monomeric species.
Richman et al. (2013). In Vitro and Mechanistic Studies of an Anti-Amyloidogenic Self-Assembled Cyclic D,L-#-Peptide Architecture. J. Americal Chemical Societ, Jan 19.Lindhagen-Persson et al. (2010). Amyloid-\x{03b2} Oligomer Specificity Mediated by the IgM Isotype \x{2013} Implications for a Specific Protective Mechanism Exerted by Endogenous Auto-Antibodies. PLoS ONE.
Product Type:
Antibody
Antibody Type:
Monoclonal
Format:
Lyophilized
Storage Temp:
Non-diluted antibody is stable for 4 years at 2-8°C. For storage at -20°C dilute antibody solution with an equal volume of glycerol to obtain final glycerol concentration of 50 % to prevent loss of enzymatic activity. Such solution will not freeze in -20°C. If you are using a 1:5000 dilution prior to diluting with glycerol, then you would need to use a 1:2500 dilution after adding glycerol. Prepare working dilution prior to use and then discard. Be sure to mix well but without foaming.
Host Animal:
Mouse
Species Reactivity:
Human Abeta oligomers only
Expected Species:
Rat
Immunogen:
partly aggregated, recombinant peptide corresponding to the human Abeta (1-40). Amino acid sequence: D-A-E-F-R-H-D-S-G-Y-E-V-H-H-Q-K-L-V-F-F-A-E-D-V-G-S-N-K-G-A-I-I-G-L-M-V-G-G-V-V
OMAB antibody is a versatile tool within research of Alzheimer\x{2019}s disease. A sandwhich ELISA illustrates its potential regarding its high selectivity towards A\x{03b2} oligomers.
Clone number:
IgM
Application Details:
Coating antibody at 2 µg/ml (ELISA), 1 : 500 (IHC)
Purity:
Affinity purified
Reconstitution:
For reconstitution add 100 µl of sterile water.
Related products:
AS13 2716 | mAB-M | human Abeta protein (3-10) region, oligomer-specific, mouse monoclonal antibodiesAS13 2715 | mAB-O | human Abeta protein (3-10) region, oligomer specific, mouse monoclonal antibodiesAgrisera matching secondary antibody: Goat anti-mouse IgM (µ chain), HRP conjugated, min. cross-reactivity to human IgG/serum, AS10 969Secondary antibodies |Amyloid beta research
Molecular Weight:
4.5 kDa
Not reactive in:
No confirmed exceptions from predicted reactivity are currently known.
Selected references:
to be added when available
Special application note:
Soluble oligomeric assemblies of the Amyloid-\x{03b2} peptide are today anticipated to be the direct cause regarding the Alzheimer pathology. As a consequence, oligomeric A\x{03b2}-assemblies constitute a very interesting therapeutic target. Identification of A\x{03b2}-oligomers is however, technically challenging due to there labile nature and low abundance. Abeta oligomer-specific OMAB antibody is based on the IgM isotype and represents a new concept of A\x{03b2}-oligomer binders using a combination of high avidity and very low monovalent affinity. This combination creates a selectivity of the antibody towards the oligomeric fraction and minimizes reactivity towards monomeric species.
Brännström et al. (2014). A Generic Method for Design of Oligomer-Specific Antibodies. PLoS ONE. DOI: 10.1371/journal.pone.0090857.
Product Type:
Antibody
Antibody Type:
Monoclonal
Format:
Lyophilized
Storage Temp:
Store lyophilized/reconstituted at -20°C; once reconstituted make aliquots to avoid repeated freeze-thaw cycles. Please, remember to spin tubes briefly prior to opening them to avoid any losses that might occur from lyophilized material adhering to the cap or sides of the tubes.
Host Animal:
Mouse
Species Reactivity:
Human
Expected Species:
Mouse, Bovine, Chicken, Dog, Porcine, Rabbit
Immunogen:
Synthetic peptide chosen from human Abeta (1-42) protein.
Applications:
Dot blot (Dot), ELISA (ELISA), Immunolocalization (IL)
Immunolocalization: human tissue was paraffin-embedded and sectioned. De-waxed and rehydrated in an ethanol gradient. Antigens were retrieved in sodium citrate buffer (pH 6) at 95°C for 1 h. The tissue sections were separately incubated for 1 h at RT with primary antibody and antibody binding was visualized with IgG Preoxidase Reagent Kit.This Monoclonal IgG1, kappa light chain, (clone number 3E5.F8) is specific for human Amyloid-Beta oligomers.
No confirmed exceptions from predicted reactivity are currently known.
Special application note:
Alzheimer's disease (AD) is the most prevalent neurodegenerative disease in the growing population of elderly people. A hallmark of AD is the accumulation of plaques in the brain of AD patients. The plaques predominantly consist of aggregates of amyloid-beta (Abeta), a peptide of 39-42 amino acids generated in vivo by specific, proteolytic cleavage of the amyloid precursor protein. Recent findings however suggest that smaller oligomeric forms of Abeta, formed in parallel to the amyloid plaques, excert the predominant tissue damaging effect.Specific identification of the oligomeric forms is as a consequence of great interest. Based on a recently published technique a highly oligomer-specific antibody (mAB-O), targeting Abeta oligomers while omitting reactivity towards the monomeric and fibrillar counterpart, has been developed.
Meilandt et al. (2019). Characterization of the selective in vitro and in vivo binding properties of crenezumab to oligomeric AÃ?². Alzheimers Res Ther. 2019 Dec 1;11(1):97. doi: 10.1186/s13195-019-0553-5.Brännström et al. (2014). A Generic Method for Design of Oligomer-Specific Antibodies. PLoS ONE. DOI: 10.1371/journal.pone.0090857.
Product Type:
Antibody
Antibody Type:
Monoclonal
Format:
Lyophilized
Storage Temp:
Store lyophilized/reconstituted at -20°C; once reconstituted make aliquots to avoid repeated freeze-thaw cycles. Please, remember to spin tubes briefly prior to opening them to avoid any losses that might occur from lyophilized material adhering to the cap or sides of the tubes.
Host Animal:
Mouse
Species Reactivity:
Human
Immunogen:
synthetic peptide chosen from human Abeta protein (3-10) pregion, oligomer specific
Applications:
Dot blot (Dot), ELISA (ELISA), Immunolocalization (IL)
No confirmed exceptions from predicted reactivity are currently known.
Selected references:
Li (2019). The Isolation of Total and Membrane-Bound Polysomes from Arabidopsis and the Detection of Their Associated AGO1 and sRNAs. Methods Mol Biol. 2019;1932:317-333. doi: 10.1007/978-1-4939-9042-9_23.You et al. (2019). FIERY1 promotes microRNA accumulation by suppressing rRNA-derived small interfering RNAs in Arabidopsis. Nat Commun. 2019 Sep 27;10(1):4424. doi: 10.1038/s41467-019-12379-z.
Special application note:
Alzheimer's disease (AD) is the most prevalent neurodegenerative disease in the growing population of elderly people. A hallmark of AD is the accumulation of plaques in the brain of AD patients. The plaques predominantly consist of aggregates of amyloid-beta (Abeta), a peptide of 39-42 amino acids generated in vivo by specific, proteolytic cleavage of the amyloid precursor protein. Recent findings however suggest that smaller oligomeric forms of Abeta, formed in parallel to the amyloid plaques, excert the predominant tissue damaging effect.Specific identification of the oligomeric forms is as a consequence of great interest. Based on a recently published technique a highly oligomer-specific antibody (mAB-M), targeting Abeta oligomers while omitting reactivity towards the monomeric and fibrillar counterpart, has been developed.
No confirmed exceptions from predicted reactivity are currently known
Special application note:
Alzheimer's disease (AD) is the most prevalent neurodegenerative disease in the growing population of elderly people. A hallmark of AD is the accumulation of plaques in the brain of AD patients. The plaques predominantly consist of aggregates of amyloid-beta (Abeta), a peptide of 39-42 amino acids generated in vivo by specific, proteolytic cleavage of the amyloid precursor protein.
No confirmed exceptions from predicted reactivity are currently known
Special application note:
Alzheimer's disease (AD) is the most prevalent neurodegenerative disease in the growing population of elderly people. A hallmark of AD is the accumulation of plaques in the brain of AD patients. The plaques predominantly consist of aggregates of amyloid-beta (Abeta), a peptide of 39-42 amino acids generated in vivo by specific, proteolytic cleavage of the amyloid precursor protein.
No confirmed exceptions from predicted reactivity are currently known
Special application note:
Alzheimer's disease (AD) is the most prevalent neurodegenerative disease in the growing population of elderly people. A hallmark of AD is the accumulation of plaques in the brain of AD patients. The plaques predominantly consist of aggregates of amyloid-beta (Abeta), a peptide of 39-42 amino acids generated in vivo by specific, proteolytic cleavage of the amyloid precursor protein.
The oligomeric form of Amyloid Beta peptide (A?, 1-42) has been closely linked to Alzheimer's Disease. Several ELISAs targeting A? have been developed; however, these ELISAs are known to cross-react with Amyloid Beta precursor protein (APP) and are poorly characterized against monomeric and oligomeric forms of the peptide. The Biosensis MOAB-2 antibody, developed by LaDu and co-workers (Youmans K. et al., 2012), has been shown to specifically detect A?, but not the precursor molecule APP. When utilized in ELISAs, the oligomeric form of A? peptide (o-A?) can be assayed independently of the other forms of the molecule when assayed with the MOAB-2 monoclonal antibody. The Biosensis oligomeric A? ELISA kit is a sandwich ELISA that allows the preferential quantification of oligomeric A? peptides. This kit is exclusive to Biosensis and consists of a pre-coated mouse monoclonal anti-A? capture antibody (MOAB-2), a biotinylated MOAB-2 detection antibody and horseradish peroxidase (HRP)-conjugated streptavidin. The addition of a substrate (3,3',5,5'-tetramethylbenzidine, TMB) yields a colored reaction product which is directly proportional to the concentration of o-A? present in samples and protein standards. The purpose of this kit is the in vitro qualitative measurement of oligomeric A? peptide levels in brain extracts and CSF samples from both transgenic mice and humans relative to a known o-A? standard. The inclusion of a highly validated oligomeric standard results in a unique, ready-to-use ELISA kit.This kit has been configured for research use only and is not to be used in diagnostic or clinical procedures.
Product Type:
ELISA
Antibody Type:
Monoclonal-Monoclonal
Format:
Ready to use Assay, complete with pre-coated plates, Concentrated Buffers, Detection reagents and complete instructions.
Storage Temp:
Store at 4 °C
Species Reactivity:
Rat
Immunogen:
The standard in this ELISA is synthetically manufactured beta-amyloid peptide, amino acids 1-42 of human, HFIP treated and dried.The stabilized oligomeric beta amyloid 1-42 control complex is also constructed from the same synthetic peptide standard material. No animal systems were used for their manufacture.
The ELISA kit box contains 1 x 96-well pre-coated strip plate, protein standards, QC sample, detection reagents, wash and sample buffers, substrate buffer and detailed protocols.
Shelf Life:
12 months from purchase.
Specificity:
Human. MOAB-2 (mouse IgG2b) is a pan-specific, high-titer antibody to A? residues 1-4 and is highly specific just to amyloid beta peptide.The Biosensis o-A? Elisa detects A? oligomers as validated and described by Youmans KL et al (2012) and Rat by Combes M et al (2015). | Rat.
References:
S Liu, S Park, G Allington, F Prelli, Y Sun, M Martá-Ariza, H Scholtzova, G Biswas, B Brown, PB Verghese, PD Mehta, Y-U Kwon and T Wisniewski (2017) "Targeting Apolipoprotein E/Amyloid ? Binding by Peptoid CPO_A?17-21 P Ameliorates Alzheimer's Disease Related Pathology and Cognitive Decline." Sci Rep. 7(1):8009 Application: ELISA, Species: Transgenic mouse brain homogenates.M Cacciottolo, X Wang, I Driscoll, N Woodward, A Saffari, J Reyes, M L Serre, W Vizuete, C Sioutas, T E Morgan, M Gatz, H C Chui, S A Shumaker, S M Resnick, M A Espeland, C E Finch and J C Chen (2017) "Particulate air pollutants, APOE alleles and their contributions to cognitive impairment in older women and to amyloidogenesis in experimental models." Transl Psychiatry. Jan 31;7(1):e1022. Application: ELISA, Species: Extracts of E3FAD and E4FAD transgenic mouse brains.Riya Thomas, Paulina Zuchowska, Alan W. J. Morris, Felecia M. Marottoli, Sangeeta Sunny, Ryan Deaton, Peter H. Gann, Leon M. Tai (2016) "Epidermal growth factor prevents APOE4 and amyloid-beta-induced cognitive and cerebrovascular deficits in female mice." Acta Neuropathol Commun. 4(1):111 Application: ELISA, Species: Tris-extracts of EFAD transgenic mouse brains.Nor Faeizah Ibrahim, Daijiro Yanagisawa, Lina Wati Durani, Hamizah Shahirah Hamezah, Hanafi Ahmad Damanhuri, Wan Zurinah Wan Ngah, Mayumi Tsuji, Yuji Kiuchi, Kenjiro Ono, Ikuo Tooyama (2016) "Tocotrienol-Rich Fraction Modulates Amyloid Pathology and Improves Cognitive Function in A?PP/PS1 Mice." J Alzheimers Dis. [Epub ahead of print]. Application: ELISA, Species: Tris-extracts of mouse brain homogenates.Jia Luo, Sue H. Lee, Lawren VandeVrede, Zhihui Qin, Manel Ben Aissa, John Larson, Andrew F. Teich, Ottavio Arancio, Yohan D'Souza, Ahmed Elharram, Kevin Koster, Leon M. Tai, Mary Jo LaDu, Brian M. Bennett and Gregory R. J. Thatcher (2016) "A multifunctional therapeutic approach to disease modification in multiple familial mouse models and a novel sporadic model of Alzheimer's disease." Molecular Neurodegeneration 2016 11:35. Application: ELISA, Species: Tris-extracts of EFAD transgenic mouse brains.Weiguo Peng, Thiyagarajan M. Achariyar, Baoman Li, Yonghong Liao, Humberto Mestre, Emi Hitomi, Sean Regan, Tristan Kasper, Sisi Peng, Fengfei Ding, Helene Benveniste, Maiken Nedergaard, Rashid Dean (2016) "Suppression of glymphatic fluid transport in a mouse model of Alzheimer's disease." Neurobiology of Disease. Vol. 93, Pages 215-225 Application: ELISA, Species: TBSX-extracts of mouse cerebral cortex.Mafalda Cacciottolo, Amy Christensen, Alexandra Moser, Jiahui Liu, Christian J. Pike, Conor Smith, Mary Jo LaDu, Patrick M. Sullivan, Todd E. Morgan, Egor Dolzhenko, Andreas Charidimou, Lars-Olof Wahlund, Maria Kristofferson Wiberg, Sara Shams, Gloria Chia-Yi Chiang (2016) "The APOE4 allele shows opposite sex bias in microbleeds and Alzheimer's disease of humans and mice." Neurobiology of Aging. Volume 37, January 2016, Pages 4757 Application: ELISA, Species: Tris-extracts of E3FAD and E4FAD transgenic mouse brains.Combes M, Poindron P, Callizot N.(2015) "Glutamate protects neuromuscular junctions from deleterious effects of ?-amyloid peptide and conversely: An in vitro study in a nerve-muscle coculture." J Neurosci. Res. 93(4):633-43 Application: ELISA, Species: Native Rat neurites & human muscle cell co-culture supernatants.Seo, Dong Han, et al. (2015) "Plasma-enabled sustainable elemental lifecycles: honeycomb-derived graphenes for next-generation biosensors and supercapacitors." Green Chem. 17:2164-2171. Application: ELISA, Species: synthetic constructs.Tai, LM (2014) "Amyloid-? Pathology and APOE Genotype Modulate Retinoid X Receptor Agonist Activity in vivo." J Biol Chem. 289(44):30538-55 Application: ELISA, Species: EFAD-Tg mice.Liu Y, Liu X, Hao W, Decker Y, Schomburg R, Fülop L, Pasparakis M, Menger MD, Fassbender K. (2014) "IKKbeta Deficiency in Myeloid Cells Ameliorates Alzheimer's Disease-Related Symptoms and Pathology." (2014) J Neurosci. Sep 24;34(39):12982-99 Application: ELISA, Species: Transgenic Mouse brain lysates, supernatants.
Related Products:
Amyloid beta research | Oligomeric Human beta-Amyloid A?1-42 Peptide, Stabilized (PE-1750-1000)Beta-Amyloid A?1-42 Peptide, HFIP-treated (PE-1749-50)
The oligomeric form of Amyloid Beta peptide (A?, 1-42) has been closely linked to Alzheimer's Disease. Several ELISAs targeting A? have been developed; however, these ELISAs are known to cross-react with Amyloid Beta precursor protein (APP) and are poorly characterized against monomeric and oligomeric forms of the peptide. The Biosensis MOAB-2 antibody, developed by LaDu and co-workers (Youmans K. et al., 2012), has been shown to specifically detect A?, but not the precursor molecule APP. When utilized in ELISAs, the oligomeric form of A? peptide (o-A?) can be assayed independently of the other forms of the molecule when assayed with the MOAB-2 monoclonal antibody. The Biosensis oligomeric A? ELISA kit is a sandwich ELISA that allows the preferential quantification of oligomeric A? peptides. This kit is exclusive to Biosensis and consists of a pre-coated mouse monoclonal anti-A? capture antibody (MOAB-2), a biotinylated MOAB-2 detection antibody and horseradish peroxidase (HRP)-conjugated streptavidin. The addition of a substrate (3,3',5,5'-tetramethylbenzidine, TMB) yields a colored reaction product which is directly proportional to the concentration of o-A? present in samples and protein standards. The purpose of this kit is the in vitro qualitative measurement of oligomeric A? peptide levels in brain extracts and CSF samples from both transgenic mice and humans relative to a known o-A? standard. The inclusion of a highly validated oligomeric standard results in a unique, ready-to-use ELISA kit. This kit has been configured for research use only and is not to be used in diagnostic or clinical procedures.
Product Type:
ELISA
Antibody Type:
Monoclonal-Monoclonal
Format:
Ready to use Assay, complete with pre-coated plates, Concentrated Buffers, Detection reagents and complete instructions.
Storage Temp:
Store at 4 °C
Species Reactivity:
Rat
Immunogen:
The standard in this ELISA is synthetically manufactured beta-amyloid peptide, amino acids 1-42 of human, HFIP treated and dried.The stabilized oligomeric beta amyloid 1-42 control complex is also constructed from the same synthetic peptide standard material. No animal systems were used for their manufacture.
The ELISA kit box contains 2 x 96-well pre-coated strip plates, protein standards, QC sample, detection reagents, wash and sample buffers, substrate buffer and detailed protocols.
Shelf Life:
12 months from purchase.
Specificity:
Human. MOAB-2 (mouse IgG2b) is a pan-specific, high-titer antibody to A? residues 1-4 and is highly specific just to amyloid beta peptide. The Biosensis o-A? Elisa detects A? oligomers as validated and described by Youmans KL et al (2012) and Rat by Combes M et al (2015). | Rat.
References:
S Liu, S Park, G Allington, F Prelli, Y Sun, M Martá-Ariza, H Scholtzova, G Biswas, B Brown, PB Verghese, PD Mehta, Y-U Kwon and T Wisniewski (2017) "Targeting Apolipoprotein E/Amyloid ? Binding by Peptoid CPO_A?17-21 P Ameliorates Alzheimer's Disease Related Pathology and Cognitive Decline." Sci Rep. 7(1):8009 Application: ELISA, Species: Transgenic mouse brain homogenates.M Cacciottolo, X Wang, I Driscoll, N Woodward, A Saffari, J Reyes, M L Serre, W Vizuete, C Sioutas, T E Morgan, M Gatz, H C Chui, S A Shumaker, S M Resnick, M A Espeland, C E Finch and J C Chen (2017) "Particulate air pollutants, APOE alleles and their contributions to cognitive impairment in older women and to amyloidogenesis in experimental models." Transl Psychiatry. Jan 31;7(1):e1022. Application: ELISA, Species: Extracts of E3FAD and E4FAD transgenic mouse brains.Riya Thomas, Paulina Zuchowska, Alan W. J. Morris, Felecia M. Marottoli, Sangeeta Sunny, Ryan Deaton, Peter H. Gann, Leon M. Tai (2016) "Epidermal growth factor prevents APOE4 and amyloid-beta-induced cognitive and cerebrovascular deficits in female mice." Acta Neuropathol Commun. 4(1):111 Application: ELISA, Species: Tris-extracts of EFAD transgenic mouse brains.Nor Faeizah Ibrahim, Daijiro Yanagisawa, Lina Wati Durani, Hamizah Shahirah Hamezah, Hanafi Ahmad Damanhuri, Wan Zurinah Wan Ngah, Mayumi Tsuji, Yuji Kiuchi, Kenjiro Ono, Ikuo Tooyama (2016) "Tocotrienol-Rich Fraction Modulates Amyloid Pathology and Improves Cognitive Function in A?PP/PS1 Mice." J Alzheimers Dis. [Epub ahead of print]. Application: ELISA, Species: Tris-extracts of mouse brain homogenates.Jia Luo, Sue H. Lee, Lawren VandeVrede, Zhihui Qin, Manel Ben Aissa, John Larson, Andrew F. Teich, Ottavio Arancio, Yohan D'Souza, Ahmed Elharram, Kevin Koster, Leon M. Tai, Mary Jo LaDu, Brian M. Bennett and Gregory R. J. Thatcher (2016) "A multifunctional therapeutic approach to disease modification in multiple familial mouse models and a novel sporadic model of Alzheimer's disease." Molecular Neurodegeneration 2016 11:35. Application: ELISA, Species: Tris-extracts of EFAD transgenic mouse brains.Weiguo Peng, Thiyagarajan M. Achariyar, Baoman Li, Yonghong Liao, Humberto Mestre, Emi Hitomi, Sean Regan, Tristan Kasper, Sisi Peng, Fengfei Ding, Helene Benveniste, Maiken Nedergaard, Rashid Dean (2016) "Suppression of glymphatic fluid transport in a mouse model of Alzheimer's disease." Neurobiology of Disease. Vol. 93, Pages 215-225 Application: ELISA, Species: TBSX-extracts of mouse cerebral cortex.Mafalda Cacciottolo, Amy Christensen, Alexandra Moser, Jiahui Liu, Christian J. Pike, Conor Smith, Mary Jo LaDu, Patrick M. Sullivan, Todd E. Morgan, Egor Dolzhenko, Andreas Charidimou, Lars-Olof Wahlund, Maria Kristofferson Wiberg, Sara Shams, Gloria Chia-Yi Chiang (2016) "The APOE4 allele shows opposite sex bias in microbleeds and Alzheimer's disease of humans and mice." Neurobiology of Aging. Volume 37, January 2016, Pages 4757 Application: ELISA, Species: Tris-extracts of E3FAD and E4FAD transgenic mouse brains.Combes M, Poindron P, Callizot N.(2015) "Glutamate protects neuromuscular junctions from deleterious effects of ?-amyloid peptide and conversely: An in vitro study in a nerve-muscle coculture." J Neurosci. Res. 93(4):633-43 Application: ELISA, Species: Native Rat neurites & human muscle cell co-culture supernatants.Seo, Dong Han, et al. (2015) "Plasma-enabled sustainable elemental lifecycles: honeycomb-derived graphenes for next-generation biosensors and supercapacitors." Green Chem. 17:2164-2171. Application: ELISA, Species: synthetic constructs.Tai, LM (2014) "Amyloid-? Pathology and APOE Genotype Modulate Retinoid X Receptor Agonist Activity in vivo." J Biol Chem. 289(44):30538-55 Application: ELISA, Species: EFAD-Tg mice.Liu Y, Liu X, Hao W, Decker Y, Schomburg R, Fülop L, Pasparakis M, Menger MD, Fassbender K. (2014) "IKKbeta Deficiency in Myeloid Cells Ameliorates Alzheimer's Disease-Related Symptoms and Pathology." (2014) J Neurosci. Sep 24;34(39):12982-99 Application: ELISA, Species: Transgenic Mouse brain lysates, supernatants.
Related Products:
Amyloid beta research | Oligomeric Human beta-Amyloid A?1-42 Peptide, Stabilized (PE-1750-1000)Beta-Amyloid A?1-42 Peptide, HFIP-treated (PE-1749-50)
The amyloid beta peptide is derived from the cleavage of the Amyloid precursor protein (APP) and varies in length from 39 to 43 amino acids. However, the form(s) of amyloid-beta peptide (A?) associated with the pathology characteristic of Alzheimer's disease (AD) remains unclear. In particular, the neurotoxicity of intraneuronal A? accumulation is an area of considerable research and controversy principally because antibodies thought to be specific for A? have been shown to actually detect intraneuronal APP and not A? exclusively.MOAB-2 (mouse IgG2b) is a pan-specific, high-titer antibody to A? residues 1-4 as demonstrated by biochemical and immunohistochemical analyses (IHC), and is highly specific just to amyloid beta peptide.MOAB-2 did not detect APP or APP-CTFs in cell culture media/lysates (HEK-APPSwe or HEK APPSwe/BACE1) or in brain homogenates from transgenic mice expressing 5 familial AD (FAD) mutation (5xFAD mice). Using IHC on 5xFAD brain tissue, MOAB-2 immunoreactivity co-localized with C-terminal antibodies specific for A?40 and A?42. MOAB-2 did not co-localize with either N- or C-terminal antibodies to APP. In addition, no MOAB-2-immunreactivity was observed in the brains of 5xFAD/BACE-/- mice, although significant amounts of APP were detected by N- and C-terminal antibodies to APP, as well as by 6E10.In both 5xFAD and 3xTg mouse brain tissue, MOAB-2 co-localized with cathepsin-D, a marker for acidic organelles, further evidence for intraneuronal A?, distinct from A? associated with the cell membrane. MOAB-2 demonstrated strong intraneuronal and extra-cellular immunoreactivity in 5xFAD and 3xTg mouse brain tissues.
Product Type:
Antibody
Antibody Type:
Monoclonal
Format:
Lyophilized, from a Protein A purified preparation in 0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, 0.01% sodium azide, pH 7.2; contains 0.01% sodium azide as a preservative.
Storage Temp:
After reconstitution keep aliquots at -20 ° to -70C for a higher stability. At 4 °C keep up to one week, insulated, protected from light; use sterile methods and pipettes. Highly purified glycerol (1:1) may be added for an additional stability. Avoid repetitive freeze/thaw cycles. Keep tightly closed when not in use and protected from light.
Host Animal:
Mouse
Species Reactivity:
Human, Rat
Immunogen:
Recombinant human amyloid beta protein 42 (A?42): DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA
Western Blotting (WB), Immunohistochemistry (IH), Immunohistochemistry/paraffin embedded IH(P), Immunoprecipitation (IP), Immunofluorescence (IF), ELISA.Antibody has been tested in WB using purified synthetic beta-amyloid preparations and from transgenic mouse brain formic acid extracts (see figure 1). Formic acid extraction/concentration is required for western blot detection from extracts. MOAB-2 antibody is specific for beta-amyloid and does not detect APP. Suggested dilution of 1:2000-1:5,000 for WB, standard ECL detection systems. Tissue samples for the detection of beta-amyloid should be prepared as detailed in K.L. Youmans et al. {Journal of Neuroscience Methods 196 (2011) 5159} for best results. Detection of beta-amyloid 40/42 in direct westerns can be difficult; Dot-blots of prepared samples are recommended as detailed in Youmans. KL et al 2012. IR or fluorescent detection systems not yet tested, they but are expected to work well with higher primary antibody dilutions because of the increased sensitivity of the detection methods.Suggested dilutions for IHC are 1:50-1:1,000. Fresh frozen, 4% paraformaldehyde fixed frozen, or formalin fixed paraffin embedded tissues are all suitable. Optimal dilutions must be determined by the end user. Antigen retrieval is required in fixed tissues for optimal staining.Antibody was tested on 4% paraformaldehyde/0.1% glutaraldehyde fixed frozen tissue from 3xTg and 5xFAD mice. MOAB-2 antibody detects intraneuronal and extracellular beta-amyloid in IHC and does not detect APP {Youmans KL et al 2012}. The antibody also reacts with archival formalin-fixed, paraffin-embedded tissue samples with antigen Heat Induced Epitope Retrieval (HIER): Recommended Citrate, pH 6.0 buffer for HIER. Signal was weak without antigen retrieval. Immunoreactively was expressed in intraneural-amyloid deposition (plaque) in Alzheimer's brain. MoAB-2 was found to be extremely clean and with an excellent signal to noise ratio with no neuro-cellular diffusive staining.In addition MOAB-2 demonstrated no significant differences in A? detection using paraffin fixed, free-floating sections {Youmans KL et al 2012}. Formic acid (FA) treatment resulted in optimal detection of both intraneuronal and extracellular A? compared to without FA (incubated in 88% FA 8 min, Youmans KL et al 2012). Free floating tissue sections were permeabilized in TBS containing 0.25% Triton X-100 (TBSX; 3 Ã 10 min), blocked with 3% horse serum in TBSX (3 Ã 10 min) followed by 1% horse serum in TBSX (2 Ã10 min) and incubated with appropriate primary antibodies diluted in TBSX containing 1% horse serum overnight. See Youmans KL et al 2012 for full IH(P) protocol and method details. For IF, suggested dilution is 1:100-1:500. The antibody was tested on 4% PFA fixed frozen tissue. Fixed tissues were washed in TBS (3 Ã 10 min), then incubated in 88% FA (8 min), and then permeabilized in TBSX (3 Ã 10 min), and blocked in TBSX containing 5% bovine serum albumin (BSA; 1 hr). Sections were subsequently incubated with appropriate primary antibodies diluted in TBSX containing 2% BSA overnight on an oscillatory rotator. Detection was via fluorescently labelled absorbed secondary antibodies {Youmans KL et al 2012}.For IP, the suggested dilution is 1:200 to 1:1,000 for labeled beta-amyloid using Protein A/G conjugated beads as the capture vehicle {Youmans KL et al 2012}.In an ELISA, a dilution of 1:50-1:1000 is suggested. The antibody has been tested in ELISAs on synthetic beta-amyloid and tissue homogenates from beta-amyloid-Tg mice. Biosensis recommends optimal dilutions/concentrations should be determined by the end user for all applications. Dilutions provided are only meant to serve as a basic guide.
Alternative Names:
Beta-APP42; Beta-APP40; Beta-amyloid protein 42; Beta-amyloid protein 40; ABPP; APPI; Amyloid beta A4 protein;MOAB2;MOAB-2; Alzheimer's antibody;AB40;AB42;abeta
Accession Number:
P05067 A4_HUMAN;
Reconstitution:
Reconstitute in 100 µL of sterile water. Centrifuge to remove any insoluble material. Final buffer is 0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, 0.01% sodium azide, pH 7.2.
Shelf Life:
12 months after purchase
Specificity:
MOAB-2 detects preparations enriched in U-, O-, F-A?42, and U-A?40 by dot-blot, and is thus a pan-specific A? antibody. However, MOAB-2 is selective for the more neurotoxic A?42 compared to A?40. Indeed, MOAB-2 demonstrated a titration against antigen concentration, and detects A?40 at 2.5 pmol but U-, O- and FA?b42 at antigen concentrations as low as ~ 0.1 pmol {Youmans. KL et al 2012}. MOAB-2 does not detect APP (Amyloid precursor protein). | Human, Rat, other species not yet tested.By Dot blot, MOAB-2 detected rat A?40 and human A?40, albeit with less affinity than for A?42. {Youmans. KL et al 2012}
References:
Zhu, B. et al. (2017) ER-associated degradation regulates Alzheimer's amyloid pathology and memory function by modulating γ-secretase activity. Nat Commun. 8(1):1472. Application: IHCHuang, TY. et al. (2017) SORLA attenuates EphA4 signaling and amyloid ?induced neurodegeneration. J Exp Med. pii: jem.20171413. [Epub ahead of print]. Application: IHCFelecia, M. et al. (2017) Peripheral Inflammation, Apolipoprotein E4, and Amyloid-? Interact to Induce Cognitive and Cerebrovascular Dysfunction. ASN Neuro. 9(4):1759091417719201. Application: IHC/IFThomas, R. et al. (2016) Epidermal growth factor prevents APOE4 and amyloid-beta-induced cognitive and cerebrovascular deficits in female mice. Acta Neuropathol Commun. 4(1):111 Application: IHCKoster, KP. et al. (2016) Epidermal growth factor prevents oligomeric amyloid-? induced angiogenesis deficits in vitro. J Cereb Blood Flow Metab. [Epub ahead of print] Application: IFLoffler, T. et al. (2016) Decreased Plasma A? in Hyperlipidemic APPSL Transgenic Mice Is Associated with BBB Dysfunction. Front. Neurosci. Application: IFKobro-Flatmoen, A. et al. (2016) Reelin-immunoreactive neurons in entorhinal cortex layer II selectively express intracellular amyloid in early Alzheimer's disease. Neurobiology of Disease. 93:172-183. Application: IHCTai, LM. et al. (2016) The role of APOE in cerebrovascular dysfunction. Acta Neuropathol. 131(5):709-23. Application: IFKim, YH. et al. (2015) A 3D human neural cell culture system for modeling Alzheimer's disease. Nat Prot. 10(7):985-1006. Application: WBCondello, C. et al. (2015) Microglia constitute a barrier that prevents neurotoxic protofibrillar A?42 hotspots around plaques. Nat Commun. 6:6176. Application: IFIulita MF et al (2014) Intracellular Abeta pathology and early cognitive impairments in a transgenic rat model overexpressing human amyloid precursor protein: a multidimensional study. Acta Neuropathol Commun. 6:61. Application: IF, IHSmith BR et al (2014) Neuronal inclusions of alpha-synuclein contribute to the pathogenesis of Krabbe disease. J Pathol. Apr;235(5):509-21. Application: IF
Research Areas:
Biosensis Alzheimer's / Parkinson's
Related Products:
Amyloid beta research
Purity:
This product is a Protein A purified mouse IgGb in 0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, 0.01% sodium azide, pH 7.2.
The amyloid beta peptide is derived from the cleavage of the Amyloid precursor protein (APP) and varies in length from 39 to 43 amino acids. However, the form(s) of amyloid-beta peptide (A?) associated with the pathology characteristic of Alzheimer's disease (AD) remains unclear. In particular, the neurotoxicity of intraneuronal A? accumulation is an area of considerable research and controversy principally because antibodies thought to be specific for A? have been shown to actually detect intraneuronal APP and not A? exclusively.MOAB-2 (mouse IgG2b) is a pan-specific, high-titer antibody to A? residues 1-4 as demonstrated by biochemical and immunohistochemical analyses (IHC), and is highly specific just to amyloid beta peptide. MOAB-2 did not detect APP or APP-CTFs in cell culture media/lysates (HEK-APPSwe or HEK APPSwe/BACE1) or in brain homogenates from transgenic mice expressing 5 familial AD (FAD) mutation (5xFAD mice). Using IHC on 5xFAD brain tissue, MOAB-2 immunoreactivity co-localized with C-terminal antibodies specific for A?40 and A?42. MOAB-2 did not co-localize with either N- or C-terminal antibodies to APP. In addition, no MOAB-2-immunreactivity was observed in the brains of 5xFAD/BACE-/- mice, although significant amounts of APP were detected by N- and C-terminal antibodies to APP, as well as by 6E10. In both 5xFAD and 3xTg mouse brain tissue, MOAB-2 co-localized with cathepsin-D, a marker for acidic organelles, further evidence for intraneuronal A?, distinct from A? associated with the cell membrane. MOAB-2 demonstrated strong intraneuronal and extra-cellular immunoreactivity in 5xFAD and 3xTg mouse brain tissues.Biosensis now offers biotinylated MOAB-2 antibody allowing more flexibility in experimental design by using the biotin-avidin/streptavidin detection method. Biotinylated MOAB-2 antibody may also help to reduce background staining in difficult-to-stain tissues and increase detection sensitivity. The ability of biotinylated MOAB-2 antibody to detect amyloid beta has been validated by IHC.Purified, non-biotinylated MOAB-2 antibody is available here.
Product Type:
Antibody
Antibody Type:
Monoclonal
Format:
Lyophilized from PBS buffer, pH 7.4; contains no preservative.
Storage Temp:
After reconstitution keep aliquots at -20 °C to -70 °C for a higher stability. At 2-8 °C keep up to one week; use sterile methods and pipettes. Highly purified glycerol (1:1) may be added for an additional stability. Avoid repetitive freeze/thaw cycles. Keep tightly closed when not in use and protected from light.
Host Animal:
Mouse
Species Reactivity:
Human, Rat
Immunogen:
Recombinant human amyloid beta protein 42 (A?42): DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA
The biotinylated MOAB-2 antibody has been tested by IHC (1:500 1:2,000 dilution) and is also expected to work in applications validated for the unlabelled antibody (M-1586-100) at same or higher dilutions: Western Blotting (WB), Immunohistochemistry (IHC), Immunohistochemistry/paraffin embedded IHC(P), Immunoprecipitation (IP), Immunofluorescence (IF), ELISA.Western Blotting:MOAB-2 has been tested in WB using purified synthetic beta-amyloid preparations and from transgenic mouse brain formic acid extracts (see Figure 1). Formic acid extraction/concentration is required for western blot detection from extracts. Suggested dilution of 1:2000-1:5,000 for WB, standard ECL detection systems. Tissue samples for the detection of beta-amyloid should be prepared as detailed in Youmans KL et al., 2011 (Journal of Neuroscience Methods 196: 5159) for best results. Detection of beta-amyloid 40/42 in direct westerns can be difficult; Dot-blots of prepared samples are recommended as detailed in Youmans KL et al., 2012. Immunohistochemistry:Suggested dilution for biotinylated MOAB-2 in IHC is 1:500-1:2,000. Fresh frozen, 4% paraformaldehyde fixed frozen, or formalin fixed paraffin embedded tissues are all suitable. Antigen retrieval is required in fixed tissues for optimal staining.Antibody was tested on 4% paraformaldehyde/0.1% glutaraldehyde fixed frozen tissue from 3xTg and 5xFAD mice. MOAB-2 antibody detects intraneuronal and extracellular beta-amyloid in IHC and does not detect APP (Youmans KL et al., 2012).The antibody also reacts with archival formalin-fixed, paraffin-embedded tissue samples with antigen Heat Induced Epitope Retrieval (HIER). Recommended buffer for HIER is citrate, pH 6.0. Signal was weak without antigen retrieval. Immunoreactivity was observed in intraneural-amyloid deposition (plaque) in Alzheimer's brain. MOAB-2 was found to be extremely clean and with an excellent signal to noise ratio with no neuro-cellular diffusive staining.In addition, MOAB-2 demonstrated no significant differences in A? detection using paraffin fixed, free-floating sections (Youmans KL et al., 2012). Formic acid (FA) treatment resulted in optimal detection of both intraneuronal and extracellular A? compared to without FA (incubated in 88% FA 8 min, Youmans KL et al., 2012). Free floating tissue sections were permeabilized in TBS containing 0.25% Triton X-100 (TBSX; 3 Ã 10 min), blocked with 3% horse serum in TBSX (3 Ã 10 min) followed by 1% horse serum in TBSX (2 Ã10 min) and incubated with appropriate primary antibodies diluted in TBSX containing 1% horse serum overnight. See Youmans KL et al., 2012, for full IHC(P) protocol and method details.Immunofluorescence:For IF, suggested dilution is 1:100-1:500. The antibody was tested on 4% PFA fixed frozen tissue. Fixed tissues were washed in TBS (3 Ã 10 min), then incubated in 88% FA (8 min), and then permeabilized in TBSX (3 Ã 10 min), and blocked in TBSX containing 5% bovine serum albumin (BSA; 1 hr). Sections were subsequently incubated with appropriate primary antibodies diluted in TBSX containing 2% BSA overnight on an oscillatory rotator. Detection was via fluorescently labelled absorbed secondary antibodies (Youmans KL et al., 2012).Immunoprecipitation:For IP, the suggested dilution is 1:200 to 1:1,000 for labelled beta-amyloid using SA-coated beads as the capture vehicle, similar to the protocols employed by Youmans KL et al., 2012.ELISA:In an ELISA, a dilution of 1:50-1:1,000 is suggested. The antibody has been tested in ELISAs on synthetic beta-amyloid and tissue homogenates from beta-amyloid-Tg mice. Biosensis recommends optimal dilutions/concentrations should be determined by the end user for all applications. Dilutions provided are only meant to serve as a basic guide.
Spin vial briefly before opening. Reconstitute in 50 µL of sterile water to give a concentration of 1 mg/mL. Centrifuge to remove any insoluble material. Final buffer is PBS, pH 7.4 without preservative.
Shelf Life:
12 months after purchase.
Specificity:
MOAB-2 detects preparations enriched in U-, O-, F-A?42, and U-A?40 by dot-blot, and is thus a pan-specific A? antibody. However, MOAB-2 is selective for the more neurotoxic A?42 compared to A?40. Indeed, MOAB-2 demonstrated a titration against antigen concentration, and detects A?40 at 2.5 pmol, but U-, O- and F-A?b42 at antigen concentrations as low as ~ 0.1 pmol (Youmans. KL et al., 2012; PMID: 22423893). MOAB-2 does not detect APP (Amyloid Precursor Protein). | Human, rat, other species not yet tested. By Dot Blot, MOAB-2 detected rat A?40 and human A?40, albeit with less affinity than for A?42 (Youmans KL et al., 2012).
References:
Ruan, CS. et al. (2017) Sortilin inhibits amyloid pathology by regulating non-specific degradation of APP. Exp Neurol. [Epub ahead of print] Application: IHCReferences for non-biotinylated MOAB-2 antibody (M-1586-100): Zhu, B. et al. (2017) ER-associated degradation regulates Alzheimer's amyloid pathology and memory function by modulating γ-secretase activity. Nat Commun. 8(1):1472. Application: IHCHuang, TY. et al. (2017) SORLA attenuates EphA4 signaling and amyloid ?induced neurodegeneration. J Exp Med. pii: jem.20171413. [Epub ahead of print]. Application: IHCFelecia, M. et al. (2017) Peripheral Inflammation, Apolipoprotein E4, and Amyloid-? Interact to Induce Cognitive and Cerebrovascular Dysfunction. ASN Neuro. 9(4):1759091417719201. Application: IHC/IFThomas, R. et al. (2016) Epidermal growth factor prevents APOE4 and amyloid-beta-induced cognitive and cerebrovascular deficits in female mice. Acta Neuropathol Commun. 4(1):111 Application: IHCKoster, KP. et al. (2016) Epidermal growth factor prevents oligomeric amyloid-? induced angiogenesis deficits in vitro. J Cereb Blood Flow Metab. [Epub ahead of print] Application: IFLoffler, T. et al. (2016) Decreased Plasma A? in Hyperlipidemic APPSL Transgenic Mice Is Associated with BBB Dysfunction. Front. Neurosci. Application: IFKobro-Flatmoen, A. et al. (2016) Reelin-immunoreactive neurons in entorhinal cortex layer II selectively express intracellular amyloid in early Alzheimer's disease. Neurobiology of Disease. 93:172-183. Application: IHCTai, LM. et al. (2016) The role of APOE in cerebrovascular dysfunction. Acta Neuropathol. 131(5):709-23. Application: IFKim, YH. et al. (2015) A 3D human neural cell culture system for modeling Alzheimer's disease. Nat Prot. 10(7):985-1006. Application: WBCondello, C. et al. (2015) Microglia constitute a barrier that prevents neurotoxic protofibrillar A?42 hotspots around plaques. Nat Commun. 6:6176. Application: IFIulita MF et al (2014) Intracellular Abeta pathology and early cognitive impairments in a transgenic rat model overexpressing human amyloid precursor protein: a multidimensional study. Acta Neuropathol Commun. 6:61. Application: IF, IHSmith BR et al (2014) Neuronal inclusions of alpha-synuclein contribute to the pathogenesis of Krabbe disease. J Pathol. Apr;235(5):509-21. Application: IF
Research Areas:
Biosensis Alzheimer's / Parkinson's
Related Products:
Amyloid beta research
Purity:
Antibody was purified from cell culture supernatant by Protein G chromatography, biotinylated and buffer-exchanged into PBS, pH 7.4 buffer
Conjugate:
Biotin
Biosensis
PE-1749-50
3 vials. 1 x 50 µg Abeta1-42 peptide; 1 x 100 µL Reconstituting Buffer, 1 x 1 mL Dilution Buffer
Synthetic beta-amyloid A?1-42 was monomerized by HFIP (hexafluoro-2-propanol) treatment and dried. One vial contains 50 µg monomeric A? peptide that can be used to form solutions of unaggregated A? monomers, aggregated A? oligomers, A? fibrils and A? protein complexes according to published protocols, and used in a variety of research applications.
Product Type:
Peptides/Controls
Format:
Lyophilized.
Storage Temp:
Store unopened, dry A? peptide vial with desiccant, insulated, at -20 °C short term, -80 °C long term. Store the buffers at 2-8 °C, do not freeze.
Preparation of unaggregated A?1-42:Important: unaggregated A? has to be prepared just prior to use!1. Add 5 µL of reconstituting buffer to one vial of 50 µg of HFIP-treated A? peptide; spin down the liquid briefly2. Vortex the vial for 5 seconds at highest speed while rotating the vial with your hands; spin down the liquid (bench-top microcentrifuge) and repeat the vortex-spin procedure for a minimum of 3 times; continue the vortex-spin procedure until all lyophilized peptide is dissolved and collected at the bottom of the tube. Important: refer to the attached instructions for a detailed procedure to ensure that all peptide is fully reconstituted!3. Add 106 µL of cold Dilution Buffer to make up to 111 µL total volume and a peptide concentration of 100 µM. Vortex-spin for 3 more times 4. Final concentration of A? is 450 µg/mL5. Use reconstituted peptide immediately to avoid oligomer formationPreparation of oligomeric A?1-42:1. Add 5 µL of reconstituting buffer to one vial of 50 µg of HFIP-treated A? peptide; spin down the liquid briefly2. Vortex the vial for 5 seconds at highest speed while rotating the vial with your hands; spin down the liquid (bench-top microcentrifuge) and repeat the vortex-spin procedure for a minimum of 3 times; continue the vortex-spin procedure until all lyophilized peptide is dissolved and collected at the bottom of the tube. Important: refer to the attached instructions for a detailed procedure to ensure that all peptide is fully reconstituted!3. Add 106 µL of cold Dilution Buffer to make up to 111 µL total volume and a peptide concentration of 100 µM4. Vortex-spin for 3 more times5. Incubate the solution at 2-8°C for 24 hours (protected from light)6. Final concentration of A? is 450 µg/mL7. Once reconstituted and oligomerized, o-A? should be used as soon as possible and within 7 days to ensure the stability of the oligomersNote: while the concentration of monomeric A? peptide used to form the oligomeric complexes is accurately determined, the precise formation, size and number of oligomers cannot be quantified by any known method.Preparation of fibrillar A?1-42:1. Add 5 µL of reconstituting buffer to one vial of 50 µg of HFIP-treated A? peptide; spin down the liquid briefly2. Vortex the vial for 5 seconds at highest speed while rotating the vial with your hands; spin down the liquid (bench-top microcentrifuge) and repeat the vortex-spin procedure for a minimum of 3 times; continue the vortex-spin procedure until all lyophilized peptide is dissolved and collected at the bottom of the tube. Important: refer to the attached instructions for a detailed procedure to ensure that all peptide is fully reconstituted!3. Add 106 µL of 10 mM HCl to make up to 111 µL total volume and a peptide concentration of 100 µM4. Vortex-spin for 3 more times 5. Incubate the solution at 37°C for 24 hours (protected from light)6. Final concentration of A? is 450 µg/mLPreparation of A?1-42 Complexes:Important: only unagreggated A? will form complexes. Use A? peptide immediately after reconstitution to form complexes.1. Add 5 µL of reconstituting buffer to one vial of 50 µg of HFIP-treated A? peptide; spin down the liquid briefly2. Vortex the vial for 5 seconds at highest speed while rotating the vial with your hands; spin down the liquid (bench-top microcentrifuge) and repeat the vortex-spin procedure for a minimum of 3 times; continue the vortex-spin procedure until all lyophilized peptide is dissolved and collected at the bottom of the tube. Important: refer to the attached instructions for a detailed procedure to ensure that all peptide is fully reconstituted!3. Add 106 µL of cold Dilution Buffer to make up to 111 µL total volume and a peptide concentration of 100 µM 4. Vortex-spin for 3 more times 5. Use reconstituted peptide immediately to avoid oligomer formation6. Mix the A? monomer with its complex partner (eg., lipoprotein) at desired concentrations in PBS, pH 7.4, or other suitable buffers compatible with its intended application7. Incubate at room temperature for 2 hours without shaking8. Use complexes immediately after incubationThese protocols are based on procedures published by Youmans KL et al., 2012 and Tai LM et al., 2013, and we refer to these publications and other relevant literature for further details.Provided working concentrations are only meant to guide the user. Optimal concentrations depend on the experimental design and need to be determined empirically.
A proprietary preparation of human amyloid beta peptide (amino acids 1-42) that was initially monomerized by HFIP-treatment and then allowed to form oligomers by the procedure described in Youmans KL et al., 2012, followed by lyophilisation using Biosensis' proprietary stabilization procedures.The resulting oligomeric mixture has been specially designed to allow the formation of stable, oligomeric A?1-42 peptide, multimeric complexes or oligomers. The material is intended to be used as a stable and consistent standard or positive control for oligomeric ELISA assays, as well as other research applications.
Product Type:
Peptides/Controls
Format:
Lyophilized, Supplied as 2 x 500 ng vials, each containing lyophilized A? oligomers. Note that the amount of provided oligomeric protein is based on the amount of monomeric A? used to form these oligomers. The precise formation, size and number of oligomers cannot be quantified by any known method.
Storage Temp:
Store unopened, lyophilized oligomeric A? with desiccant, insulated, at -20 °C short term, -80 °C long term. Store reconstituted vial at 2- 8 °C for up to 2 days. The reconstituted material should not be frozen for best results.
Use as positive control in Oligomeric A? ELISA Kit (BEK-2215): Reconstitute one vial with 1 mL of assay buffer provided in the ELISA kit. Dilute to a concentration of 0.5-1 ng/mL. At this concentration, a positive signal will be obtained within the dynamic range of the calibration curve.Use as oligomeric A-beta peptide standard in Oligomeric A? ELISA Kit (BEK-2215): Reconstitute one vial with 1 mL of assay buffer provided in the ELISA kit. Dilute to a concentration of 2 ng/mL, which represents the highest concentration of the calibration curve. Perform a 1:2 serial dilution down to 0.031 ng/mL in assay buffer. Click here for detailed instructions on generating a calibration curve with PE-1750-1000.Use as positive control in other applications: Optimal concentrations need to be determined empirically. It is recommended to reconstitute the vial with 100 200 uL buffer first (eg., PBS, pH 7.4), and prepare further working dilutions thereof.
The beta Amyloid peptide is derived from the cleavage of the Amyloid precursor protein and varies in length from 39 to 43 amino acids. Beta amyloid peptides are the major constituents of the plaques and tangles that occur in Alzheimer's disease.
Product Type:
Antibody
Antibody Type:
Polyclonal
Format:
Lyophilized
Storage Temp:
At least 12 months after purchase at 2 - 4 °C (lyophilized formulations).After reconstitution, aliquot and store at -20 °C for a higher stability and at 4 °C with an appropriate antibacterial agent. Avoid freeze-thaw cycles.
Host Animal:
Rabbit
Species Reactivity:
Human
Immunogen:
A synthetic peptide (DAEFRHDSGYEVHH) conjugated to bovine serum albumin (BSA) corresponding to amino acid sequence 1-14 of mature human beta amyloid.
Buffer contains Phosphate Buffered Saline (PBS pH 7.4). No preservatives added. Reconstitute in 100 µL of sterile water. Centrifuge to remove any insoluble material.
Shelf Life:
12 months after purchase
Specificity:
Human beta amyloid, cross reactivity to APP has not bee tested.
Amylo-Glo® RTDReady to Dilute Staining reagent is designed to stain amyloid plaques in tissue sections. This novel marker has several advantages over other conventional markers such as Thioflavin S and Congo Red because of its unique chemical and spectral properties. (L. Schmued et al. (2012) J.Neuroscience Methods 209:120 126). Using Amylo-Glo® results in a very bright blue UV excitable stain under physiological conditions that will not bleed through when illuminated with other filters. Its brightness makes it ideal for low magnification quantification studies, while its unique excitation/emission profile and mild staining conditions makes it ideal for combination for multiple immunofluorescent labeling studies. Amylo-Glo® RTDis compatible with fresh, frozen, and formalin-fixed immunohistochemistry or cytochemistry, and it is particularly good for confocal and multiple labeling because of its high fluorescent intensity and high resistance to photo-bleaching. Moreover because Amylo-Glo® fluoresces in the UV channel, double and triple labeling experiments can be performed very easily (see protocol).
Product Type:
Tracing/Staining Kit
Format:
The reagents in the Amyloid Plaque Stain Reagent (100x) are all supplied in a liquid format and are ready-to-dilute.
Storage Temp:
The stock solution can be stored for up to 6 months after date of receipt at 4 °C protected from light. No preservatives. Use sterile technique when handling and proper laboratory procedures.
Staining of amyloid plaques in human and animal tissues, see included protocol
Alternative Names:
AmyloGlo
Kit Components:
5 mL of 100X Amylo-Glo RTD (A-G RTD) solution
Reconstitution:
Ready to dilute per protocol; 100X
Shelf Life:
6 months from date of purchase
Specificity:
amyloid plaques both intraneuronal and vascular |
References:
Palombo F (2017) "Detection of A? plaque-associated astrogliosis in Alzheimer's disease brain by spectroscopic imaging and immunohistochemistry."Analyst. [Epub ahead of print] 2017; Application: IF Species: MouseAbud EM (2017) "Generation of Human Microglia from Induced Pluripotent Stem Cells to Study Innate Immunity in Neurological Diseases."PhD Thesis. 2017; Application: IF Species: MouseAbud EM et al. (2017) "iPSC-Derived Human Microglia-like Cells to Study Neurological Diseases."Neuron. 2017; 49(2):278-93 Application: IF Species: MouseSolomon IH et al. (2017) "Brain and liver pathology, amyloid deposition, and interferon responses among older HIV-positive patients in the late HAART era."BMC Infect Dis. 2017; 17(1):151 Application: IF Species: HumanXu F et al. (2016) "Cerebral vascular amyloid seeds drive amyloid ?-protein fibril assembly with a distinct anti-parallel structure."Nat Commun. 2016; 7:13527. Application: IF Species: MouseKatsouri L et al. (2016) "PPARγ-coactivator-1α gene transfer reduces neuronal loss and amyloid-? generation by reducing ?-secretase in an Alzheimer's disease model ."Proc Natl Acad Sci USA. 2016; 113(43):12292-97. Application: IF Species: MouseEsposito G et al. (2016) "Autologous transplantation of intestine-isolated glia cells improves neuropathology and restores cognitive deficits in ? amyloid-induced neurodegeneration."Sci Rep. 2016; 6: 22605. Application: IF Species: RatMarsh SE et al. (2016) "The adaptive immune system restrains Alzheimer's disease pathogenesis by modulating microglial function."Proc Natl Sci USA. Feb 16. pii: 201525466. Application: IF Species: Hu Fibrillar amyloid visualization.Kim YH et al. (2015) "A 3D human neural cell culture system for modeling Alzheimer's disease."Nat Protoc. Jul;10(7):985-1006. Application: IF Species: Hu, Human neural stem-cell-derived three-dimensional (3D) culture system.Nijholt DA et al. (2015) "Pregnancy Zone Protein is Increased in the Alzheimer's Disease Brain and Associates with Senile Plaques."J Alzheimer's Disease. 46(1):227-38. Application: IF Species: HuKamphuis W et al. (2015) "GFAP and vimentin deficiency alters gene expression in astrocytes and microglia in wild-type mice and changes the transcriptional response of reactive glia in mouse model for Alzheimer's disease."Glia. Jun;63(6):1036-56. Application: IF Species: MouseChoi SH et al. (2014) "A three-dimensional human neural cell culture model of Alzheimer's disease."Nature Oct 12. doi: 10.1038/nature1380. Application: IF Species: Hu, Human neural stem-cell-derived three-dimensional (3D) culture system.Niedowicz DM et al. (2014). "Obesity and diabetes cause cognitive dysfunction in the absence of accelerated beta-amyloid deposition in a novel murine model of mixed or vascular dementia." Acta Neuropathol Commun. 2014 Jun 10;2:64.
Related Products:
Amyloid beta research | Amylo-Glo / EB kit catalog number TR-400-AG
Purity:
Thin layer chromatography using alumina plates and a solvent system of ethanol and water (3:1) revealed the presence of two fluorescent isomers. No amount of starting material was detected.
The Biosensis AG-400-AG kit utilizes an ethidium bromide counter stain for a quick and effective way to visualize cell nuclei and cell bodies of cells while under UV illumination allowing the assessment of amyloid plaques and cell/tissue positioning as well in one step.Amylo-Glo® RTDReady to Dilute Staining reagent is designed to stain amyloid plaques in tissue sections. This novel marker has several advantages over other conventional markers such as Thioflavin S and Congo Red because of its unique chemical and spectral properties. (L. Schmued et al. (2012) J.Neuroscience Methods 209:120 126). Using Amylo-Glo® results in a very bright blue UV excitable stain under physiological conditions that will not bleed through when illuminated with other filters. Its brightness makes it ideal for low magnification quantification studies, while its unique excitation/emission profile and mild staining conditions makes it ideal for combination for multiple immunofluorescent labeling studies. Amylo-Glo® RTDis compatible with fresh, frozen, and formalin-fixed immunohistochemistry or cytochemistry, and it is particularly good for confocal and multiple labeling because of its high fluorescent intensity and high resistance to photo-bleaching. Moreover because Amylo-Glo® fluoresces in the UV channel, double and triple labeling experiments can be performed very easily (see protocol).
Product Type:
Tracing/Staining Kit
Format:
The reagents in the Amyloid Plaque Stain Reagent (100x) are all supplied in a liquid format and are ready-to-dilute.
Storage Temp:
The stock solution can be stored for up to 6 months at 4 °C protected from light. No preservatives. Use sterile technique when handling and proper laboratory procedures.
Staining of amyloid plaques in human and animal tissues, see included protocol. EtBr counter stain stains nuclei and cell bodies for easy identification and spacial orientation.
Alternative Names:
AmyloGlo
Kit Components:
1 bottle containing 40 mL of 10X Amylo-Glo® RTD (A-G RTD) solution 1 bottle containing 40 mL of 10X A-G RTD Ethidium Bromide (EtBr RTD) solution
Reconstitution:
Ready to dilute per protocol 10X solutions
Shelf Life:
6 months from date of purchase
Specificity:
amyloid plaques both intraneuronal and vascular for A-G, Etbr, nuclei and cell bodies both DNA and RNA label |
Related Products:
Amyloid beta research| TR-300-AG, MOAB-2 antibody
Purity:
Thin layer chromatography using alumina plates and a solvent system of ethanol and water (3:1) revealed the presence of two fluorescent isomers. No amount of starting material was detected.
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