Newmarket Scientific
Newmarket Scientific

Neuroscience Research

Proteins, antibodies, kits and other reagents for neuroscience

Affinity Biosciences logo   Agrisera logo     Biosensis logo   ImmunoStar logo  NS Reagents logo  



Newmarket Scientific provides products for neuroscience including:


Antibodies, Proteins, Kits and Related reagents.


Some products for neuroscience research are highlighted below, but many more are available, so please use the search box above to find other products in our neuroscience range or if there is something specific you are looking for you can email us at


Also for more information on neuroscience research in general, including highlighted articles/papers and other resources check out our .


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


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: 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


Biosensis MOAB-2 antibody to Amyloid beta peptide (40/42)

The presence of aggregated amyloid-β peptides (Aβ) is one of the hallmarks of Alzheimer's Disease (AD). However, the form(s) of Aβ-peptides that are associated with this pathology remains unclear. In particular, the neurotoxicity of intraneuronal Aβ accumulation is an area of considerable research and controversy principally because antibodies thought to be specific for Aβ have been shown to actually detect intraneuronal amyloid precursor protein (APP) and not Aβ exclusively.


Our Biosensis MOAB-2 antibody (M-1586-100) is a new pan-specific monoclonal antibody to Amyloid beta residues 1-4 and provides unparalleled staining clarity, stronger reactivity and greater sensitivity than any other Abeta monoclonal antibodies previously available for research. Also, unlike other monoclonals such as 6E10 and 4G8, MOAB-2 does not cross react with APP or APP C-terminal fragments.


The Biosensis formulation of MOAB-2 is also the only one endorsed by the original developers.


Biosensis MOAB-2 antibody to Amyloid beta peptide (A beta 40/42)


Related products:

Biosensis APP antibodies, Oligomeric Amyloid-beta ELISA Kits,

Amylo-Glo - Amyloid beta plaque staining solution


Neuroscience - ImmunoStar
Immunostar neuroscience


Newmarket Scientific is the UK and Ireland Distributor for the ImmunoStar range of antibodies for neuroscience research.


This range of primary antibodies was originally provided by DiaSorin (formerly INCSTAR), but in 2001 the range became Immunostar. As these antibodies have been available for many years there are multiple references citing their use.


Additionally ImmunoStar antibodies are put through extensive testing before release to ensure both high quality and high titer. This provides excellent reliability and lot-to-lot consistency. These antibodies have also been specifically tested for use in immunohistochemistry. 


Details of the full range of 60+ well referenced neuroscience antibodies are available on this link.


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


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.


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



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.