AB9850
Anti-phospho-α Synuclein (Ser129) Antibody
Chemicon®, from rabbit
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About This Item
UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41
Recommended Products
biological source
rabbit
Quality Level
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
purified by
affinity chromatography
species reactivity
rat
manufacturer/tradename
Chemicon®
technique(s)
western blot: suitable
NCBI accession no.
UniProt accession no.
shipped in
dry ice
target post-translational modification
phosphorylation (pSer129)
Gene Information
human ... SNCA(6622)
Specificity
Alpha Synuclein, phospho Serine 129. The antibody recognizes a protein of ~15 kDa corresponding to alpha synuclein, phospho Serine 129 in lysates from rat cortex. Immunolableing is blocked by preadsorption with the phospho-peptide used as the immunogen but not by the corresponding dephospho-peptide.
The immunogen has 100% homology with human, mouse, non-human primate, bovine and canine.
Immunogen
Synthetic peptide of amino acids surrounding the phosphoSerine 129 site of rat alpha synuclein.
Application
This Anti-phospho-α Synuclein (Ser129) Antibody is validated for use in WB for the detection of phospho-α Synuclein (Ser129).
Linkage
Replaces: 04-1052
Legal Information
CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany
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Storage Class Code
10 - Combustible liquids
WGK
WGK 2
Certificates of Analysis (COA)
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Manuela Neumann et al.
The Journal of clinical investigation, 110(10), 1429-1439 (2002-11-20)
The pathological modifications of alpha-synuclein (alphaS) in Parkinson disease and related diseases are poorly understood. We have detected misfolded alphaS in situ based on the proteinase K resistance (PK resistance) of alphaS fibrils, and using specific antibodies against S129-phosphorylated alphaS
Wanli W Smith et al.
The Journal of neuroscience : the official journal of the Society for Neuroscience, 25(23), 5544-5552 (2005-06-10)
Parkinson's disease (PD) is a neurodegenerative disorder characterized by selective loss of dopaminergic neurons and the presence of Lewy bodies. Previous reports have shown that alpha-synuclein deposited in brain tissue from individuals with synucleinopathy is extensively phosphorylated at Ser-129. Here
Effects of alpha-synuclein immunization in a mouse model of Parkinson's disease
Masliah, Eliezer, et al
Neuron, 46, 857-868 (2005)
Ningshan Wang et al.
The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society, 68(10), 669-678 (2020-09-15)
The detection of cutaneous phosphorylated alpha-synuclein (P-syn) in patients with Parkinson's disease (PD) has ranged from 30% to 100% across different studies. We hypothesize that part of the variability in P-syn detection is due to methodological differences using sections of
M Okochi et al.
The Journal of biological chemistry, 275(1), 390-397 (2000-01-05)
alpha-Synuclein has been implicated in the pathogenesis of Parkinson's disease, since rare autosomal dominant mutations are associated with early onset of the disease and alpha-synuclein was found to be a major constituent of Lewy bodies. We have analyzed alpha-synuclein expression
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