Newmarket Scientific
Newmarket Scientific








NS Reagents Antibodies (Newmarket Scientific)


The Newmarket Scientific range of antibodies


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Our NS Reagents Antibodies range includes antibodies for:

 

Neuroscience | DNA & Protein Modification | Cell signalling

 

For each of these areas we continually review the latest publications with the aim of identifying new target proteins of interest to make antibodies to. We will be developing many new antibodies each year.

 

The areas above are those we have right now, but we will be adding new research areas over time.

 

Need an antibody to a new protein... Why not get in early while we are adding to our range?

 

NS Reagents

 


If you have questions about any of our products you can contact us using the details on our contact link above.

 

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TDP43 Antibodies

TAR DNA-binding protein 43 (TDP43) binds both DNA and RNA and has multiple functions in transcriptional repression, pre-mRNA splicing and translational regulation. Characterisation of transcriptome-wide binding sites shows that thousands of RNAs are bound by TDP43 in neurons.

 

Hyperphosphorylated, fragmented and ubiquitinated forms of TDP-43 have been identified as core components of cytosolic inclusions in sporadic ALS (amyotrophic lateral sclerosis) and FTLD (frontotemporal lobar degeneration). As well as ALS and FTLD, mutations in TDP-43 have also been associated Parkinson's disease and Alzheimer's disease. 

 

TDP43 is a key target protein in research around numerous neurodegenerative conditions. Read More...

 

NS Reagents TDP43 Antibody (Cat-AA17-100105) Image 1 NS Reagents TDP43 Antibody (Cat-AA17-100105) Image 2

 

ALS patient line showing proteinopathy.

 

 

TDP43: Cat No: AX17-10010

Lot AX17-1808-0002

Technique: ICC

Secondary Ab: Alexa 488

Primary Ab dilution: 1:200

 


 

Affinity TDP43 Phospho (Cat-AF7365) Image 3 Affinity TDP43 Phospho (Cat-AF7365) Image 2

 

ALS patient line showing

nuclear TDP43 phosphorylation.

 

Affinity - phospho TDP43 Ab Cat No: AF7365

Lot 19p1575

Technique: ICC

Secondary Ab: Alexa 488

Primary Ab dilution: 1:100

 


Images courtesy of Dr Laura Ferraiuolo and Mr Marco Destro at the University of Sheffield

 



CYP46A1: a key enzyme controlling brain cholesterol levels

Cholesterol is an important cell membrane component which in the brain is found mainly in glial cells and neurons and in the myelin sheaths. Cholesterol does not usually cross the blood-brain-barrier and as a result must be synthesised in situ in the brain, transported between the various cells and then eliminated in order to maintain appropriate levels.

 

Key to maintaining brain cholesterol homeostasis is the CNS-specific cytochrome P450 enzyme Cholesterol 24-hydroxylase (CYP46A1). This cytochrome P450 enzyme which is mostly expressed in the brain (and to a lesser extent in the retina) helps eliminate excess cholesterol by converting it to 24S-hydroxycholesterol (24HC) which is membrane permeable so it can cross the blood-brain-barrier and reach the systemic circulation where it is further degraded to bile acids once in the liver.

 

Dysregulation of the activity of CYP46A1 induces changes in the cholesterol levels, which may contribute to the development of neurodegenerative diseases such as Alzheimer's and Huntington’s diseases. In Alzheimer’s disease there is significant CYP46A1 expression in astrocytes and around amyloid plaques and increasing evidence suggests that CYP46A1 has a role in the pathogenesis and progression of neurodegenerative disorders, with increasing CYP46A1 levels in the brain being neuroprotective in Huntington’s disease.

 


Related products:

NS reagents: Anti-CYP46A1 antibody

Applications: WB IHC Reactivity: Hu Ms Rt


Other CYP46A1 antibodies

 

NS reagents: Anti-CYP7B1 Antibody (Cytochrome P450 7B1/cholesterol 7 alpha-hydroxylase)

Applications: ELISA IHC WB Reactivity: Hu

 
References:

A Crosstalk Between Brain Cholesterol Oxidation and Glucose Metabolism in Alzheimer’s Disease, Gamba P et al, Front Neurosci. 2019; 13: 556. Published online 2019 May 31 


Cholesterol 24-Hydroxylation by CYP46A1: Benefits of Modulation for Brain Diseases, Petrov A M et al, Neurotherapeutics. 2019 Apr 18. doi: 10.1007/s13311-019-00731-6.

 



RNA-binding Proteins and Stress granules in ALS-FTD

Cytoplasmic stress granules are membrane-less aggregates that form through liquid phase separation as a protective response to physiological or pathological conditions such as oxidative stress, hypoxia or virus infection. They are transient and usually disappear after the stress is removed.

 

Stress granules are mainly composed of messenger RNAs (mRNAs) stalled in translation initiation, translation initiation components such as eukaryotic initiation factor 4G (eIF4G), RNA-binding proteins (RBPs) and ribonucleoproteins. Formation of stress granules can be initiated by the Ras GTPase-activating protein-binding protein 1 (G3BP1), which is commonly used as a stress granule marker.

 

Mutations in genes that encode RNA binding proteins (RBPs) such as FUS/TLS, TDP-43, Ataxin 2, TAF15, EWSR1, hnRNPA1 and hnRNPA2, MATR3 and TIA-1 have recently been linked to ALS/FTD. Some of these RNA binding proteins contain low complexity sequence domains (LCDs) that have been shown to mediate the phase separation. Mutations found in these domains increase the propensity of RNA binding proteins to aggregate and form pathological amyloid-like fibrils in the cell bodies.

 

Related products:

USP10   Caprin1    HDAC6    eIF4A3

 

TDP43 - TAR DNA-binding protein 43: A key protein in ALS and FTLD, Parkinson's and Alzheimer's 

 

References:

References: RNA-Binding Proteins in Amyotrophic Lateral Sclerosis, Zhao M. et al.

Mol Cells. 2018 Sep 30;41(9):818-829  

 

Decoding ALS: From Genes to Mechanism, Taylor JP et al.

Nature. 2016 Nov 10; 539(7628): 197–206.

 

Relationships between Stress Granules, Oxidative Stress, and Neurodegenerative Diseases Chen L et al.  Oxidative Medicine and Cellular Longevity, Volume 2017, Article ID 1809592

 



The role of the retromer component VPS-35 in neurodegenerative diseases

Cargoes, originating from the plasma membrane or the biosynthesis pathways and entering the endosomal systems, are either retained in endosomes for subsequent lysosomal degradation or are exported from the endosomes for reuse or recycling. Endosomes are therfore important protein sorting stations contributing to cell homeostasis and deficiencies in the endosomal sorting system have been linked to neurodegenerative diseases such as Alzheimer’s and Parkinson’s.

 

Retromer is an evolutionarily conserved endosomal-associated-protein known to play an essential role in the retrograde transport of transmembrane proteins from the endosomes back to the trans-Golgi network or to the plasma membrane via the recycling pathway. Retromer is a pentameric complex composed of a cargo-selective trimeric complex, with the major subunit being VPS-35 (vacuolar protein sorting 35) which is combined with a sorting nexin dimer.

 

The endosomal retromer is known to bind to and recruit the Wiskott–Aldrich syndrome and SCAR homolog (WASH) complex to the endosomal membranes. The latter helps the formation of actin patches that facilitate protein sorting. It is thought that mutations in the VPS-35 gene weaken the binding of VPS-35 with an element of the WASH complex, which consequently results in the abnormal protein sorting. The D620N mutation in VPS-35 has been associated with Parkinson’s disease.


NS Reagents VPS-35 antibodies:

NS Reagents Anti-VPS35 antibody AB19-10109

Applications: WB | IHC Reactivity: Hu | Ms

 

NS Reagents Anti-VPS35 antibody AB19-10110 (N Terminal)

Applications: WB Reactivity: Hu | Ms | Rt

 

References:

Parkinson’s disease-linked D620N VPS35 knockin mice manifest tau neuropathology and dopaminergic neurodegeneration, Chen X et al, Proc Natl Acad Sci U S A. 2019 Mar 19; 116(12): 5765–5774. 


The functional roles of retromer in Parkinson's disease, Cui Y et al, FEBS Lett. (2018) 


The retromer complex – endosomal protein recycling and beyond Seaman M.N. J, J Cell Sci. 2012 Oct 15; 125(20): 4693–4702. doi: 10.1242/jcs.103440 


Retromer: A Master Conductor of Endosome Sorting, Burd C et al, Cold Spring Harb Perspect Biol. 2014 Feb; 6(2): a016774. doi: 10.1101/cshperspect.a016774 


Retromer-mediated endosomal protein sorting: all WASHed up! Seaman MNJ et al, Trends Cell Biol. 2013 Nov;23(11):522-8. doi: 10.1016/j.tcb.2013.04.010. Epub 2013 May 28. 

 



Anti-RAMP Antibodies (1, 2 and 3)

 

Receptor Activity Modifying Proteins (RAMPs) are required to transport calcitonin-receptor-like receptor (CRLR or CALCRL) to the plasma membrane. CRLR is a G protein-coupled receptor receptor with seven transmembrane domains, which can function as either a calcitonin-gene-related peptide (CGRP) receptor or an adrenomedullin receptor, depending on which members of the RAMP family are expressed. 

 

Wth RAMP1 it produces a CGRP receptor with RAMP2 it produces an adrenomedullin (AM) receptor (AM1) with RAMP3 it produces a dual CGRP/AM receptor (AM2)

 

In general four roles have been reported for RAMPs:

1. RAMPs enable the forward-trafficking of some GPCRs to the cell surface.

2. RAMPs can alter GPCR pharmacology, switching ligand selectivity for some GPCRs.

3. RAMPs can influence coupling to GPCR signaling pathways.

4. RAMPs may alter the trafficking pathway of some GPCRs from the cell surface, with different RAMPs controlling receptor fate through recycling or degradative pathways.

 

We have 3 antibodies available as follows:

 

Anti-RAMP1 Antibody         

Applications: WB, IHC  

Host: Rabbit     Reactivity: Human, Mouse, Rat  

 

Anti-RAMP2 Antibody         

Applications: WB  

Host: Rabbit     Reactivity: Human, Mouse, Rat  

 

Anti-RAMP3 Antibody         

Applications: WB, IF  

Host: Rabbit     Reactivity: Human, Mouse, Rat  

 

All are available as 50ug or 100ug size

 

More information is available on the links above or complete the form below to request copies of the datasheets.

 


 

Anti-DNA damage-binding protein 1

 

DNA damage-binding protein 1 (DDB1) is the large subunit (p127) of the heterodimeric DNA damage-binding (DDB) complex. DDB1 also functions as a core component of the cullin 4 (CUL4) ubiquitin E3 ligase complex, facilitating the binding of substrates to this complex and the ubiquitination of proteins. These factors (ubiquitin ligase substrates) regulate numerous essential processes in the cell including DNA repair (DDB2), DNA replication, chromatin remodelling (Cdt2) and more.

 

Applications: WB           Host: Rabbit      Reactivity: Human

 



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