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AB9850

Sigma-Aldrich

Anti-phospho-α Synuclein (Ser129) Antibody

Chemicon®, from rabbit

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About This Item

Code UNSPSC :
12352203
eCl@ss :
32160702
Nomenclature NACRES :
NA.41

Source biologique

rabbit

Niveau de qualité

Forme d'anticorps

affinity isolated antibody

Type de produit anticorps

primary antibodies

Clone

polyclonal

Produit purifié par

affinity chromatography

Espèces réactives

rat

Fabricant/nom de marque

Chemicon®

Technique(s)

western blot: suitable

Numéro d'accès NCBI

Numéro d'accès UniProt

Conditions d'expédition

dry ice

Modification post-traductionnelle de la cible

phosphorylation (pSer129)

Informations sur le gène

human ... SNCA(6622)

Spécificité

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.

Immunogène

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).

Liaison

Replaces: 04-1052

Informations légales

CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany

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Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 2


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

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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