AB5336P
Anti-Synuclein α Antibody
Chemicon®, from sheep
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About This Item
UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41
Recommended Products
biological source
sheep
Quality Level
antibody form
affinity purified immunoglobulin
antibody product type
primary antibodies
clone
polyclonal
purified by
affinity chromatography
species reactivity
rat, mouse, human
manufacturer/tradename
Chemicon®
technique(s)
immunohistochemistry: suitable (paraffin)
NCBI accession no.
UniProt accession no.
shipped in
dry ice
target post-translational modification
unmodified
Gene Information
human ... SNCA(6622)
Immunogen
Synthetic peptide corresponding amino acids 108-120 of human alpha synuclein.
Application
Anti-Synuclein Antibody, α is an antibody against Synuclein for use in IH(P).
Immunohistochemistry: 1:1,000 on frozen or paraffin sections.
Optimal working dilutions must be determined by the end user.
Optimal working dilutions must be determined by the end user.
Linkage
Replaces: 04-1053
Physical form
Affinity purified immunoglobulin. Lyophilized. Reconstitute with 50 μL of sterile distilled water. Centrifuge to remove any residue. Glycerol (1:1) can be added for additional stability.
Legal Information
CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany
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Description
Pricing
Hazard Statements
Precautionary Statements
Hazard Classifications
Aquatic Chronic 3
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Certificates of Analysis (COA)
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Mohamed-Bilal Fares et al.
Proceedings of the National Academy of Sciences of the United States of America, 113(7), E912-E921 (2016-02-04)
Lewy bodies (LBs) are intraneuronal inclusions consisting primarily of fibrillized human α-synuclein (hα-Syn) protein, which represent the major pathological hallmark of Parkinson's disease (PD). Although doubling hα-Syn expression provokes LB pathology in humans, hα-Syn overexpression does not trigger the formation
Avik Roy et al.
Scientific reports, 6, 22067-22067 (2016-02-27)
Ankyrin-rich BTB/POZ domain containing protein-2 or BPOZ-2, a scaffold protein, has been recently shown to control the degradation of many biological proteins ranging from embryonic development to tumor progression. However, its role in the process of neuronal diseases has not
Ayse Ulusoy et al.
The European journal of neuroscience, 32(3), 409-422 (2010-08-14)
Lewy bodies, which are a pathological hallmark of Parkinson's disease, contain insoluble polymers of alpha-synuclein (alphasyn). Among the different modifications that can promote the formation of toxic alphasyn species, C-terminal truncation is among the most abundant alterations in patients with
Martial Kamdem Mbefo et al.
The Journal of biological chemistry, 290(15), 9412-9427 (2015-02-07)
Although α-synuclein (α-syn) phosphorylation has been considered as a hallmark of sporadic and familial Parkinson disease (PD), little is known about the effect of PD-linked mutations on α-syn phosphorylation. In this study, we investigated the effects of the A30P, E46K
Cristiane Latge et al.
The Journal of biological chemistry, 290(33), 20527-20540 (2015-07-08)
Cerebral dopamine neurotrophic factor (CDNF) is a promising therapeutic agent for Parkinson disease. As such, there has been great interest in studying its mode of action, which remains unknown. The three-dimensional crystal structure of the N terminus (residues 9-107) of
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