Newmarket Scientific
Newmarket Scientific


Proteins, antibodies, kits and other reagents for neuroscience

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



Newmarket Scientific provides products for neuroscience including:


Antibodies, Proteins, Immunohistochemistry kits and Related reagents.


Please visit our immunohistochemistry page for details of our IHC kits or if you are having difficulty locating an item, simply use our contact form and we'll look for you.


More information on neuroscience research including highlighted papers and other resources is available on our Exosome Twitter feed:


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


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.


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:






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


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 is synthesised in situ in the brain, transported between the various cells and then eliminated in order to maintain appropriate levels.


CYP46A1 is a CNS-specific cytochrome P450 enzyme which is mostly expressed in the brain and to a lesser extent in the retina. CYP26A1 helps eliminate excess cholesterol by converting it to 24S-hydroxycholesterol (24HC). 24HC 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.


Related products:

NS reagents anti-CYP46A1 antibody AB19-10097

Applications: WB IHC Reactivity: Hu Ms Rt

Other CYP46A1 antibodies


NS reagents: CYP7B1 AX17-10008 (In development)

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.


StressMarq New Active Preformed Fibrils and Filaments for Neurodegeneration research

StressMarq has recently released new proteins for the study of neurodegenerative diseases including alpha synuclein, beta synuclein, gamma synuclein, tau, SOD1 and TTR.


Protein conformation disorders such as alpha-synucleinopathies, tauopathies, ALS and amyloidosis are characterised by the assembly of normally soluble proteins into insoluble aggregates. The use of the “preformed fibril model” where monomers are converted into preformed fibrils is gaining popularity amongst researchers to study neurodegenerative disorders such as Parkinson’s and Alzheimer’s.


Preformed fibrils can be used in vitro, adding them to the culture media or in vivo injecting them into the brain. Although pathological preformed fibrils can be generated from monomers, not all preformed fibrils formed are able to seed inclusions in cells/neurons.


However StressMarq has produced a wide range of already validated active preformed fibrils and monomers that produce consistent pathology (validated protein concentration, sedimentation assay, thioflavin T assay, electron microscopic visualisation of the fibrils) . These active preformed fibrils induce protein aggregation/biological activities both in vitro and in vivo.


Protocols: Cell Culture Assay, ASYN Thioflavin T Assay.



Alpha Synuclein Preformed Fibrils    Beta Synuclein Preformed Fibrils    Gamma Synuclein Preformed Fibrils

TTR Preformed Fibrils    SOD1 Preformed Fibrils    Tau Preformed Fibrils


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/ “recycling”. Endosomes are hence important proteins sorting stations contributing to cell homeostasis and deficiencies in the endosomal sorting system has been linked to neurodegenerative diseases such as Alzheimer’s and Parkinson’s.


Retromer, an evolutionary conserved endosomal-associated-protein, is 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. It is a pentameric complex composed of a cargo-selective trimeric complex, with vacuolar protein sorting 35 (VPS-35) being the major subunit, and of a sortin 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, consequently resulting in the abnormal sorting of the cargo. The D620N mutation in VPS-35 has been associated with Parkinson’s disease.

NS Reagents VPS-35 antibodies:


Anti-VPS35 antibody AB19-10109 (synthetic peptide)

Applications: WB | IHC Reactivity: Hu | Ms


Anti-VPS35 antibody AB19-10110

Applications: WB Reactivity: Hu | Ms | Rt


StressMarq VPS-35 antibody [7E4] SMC-602D

Applications: WB| ICC/IF Reactivity: Hu | Ms


VPS Antibody Image

A) VPS35 KO A549 cells B) WT A549 cells.

Courtesy of: Dario Alessi Lab, University of Dundee.


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.