Synuclein, alpha (Non A4 Component of Amyloid Precursor) (SNCA) (Tyr125) antibody
Alternatives Western Blotting (WB)
|5 references available|
|Quantity||0.1 mg (0.5 mg/ml)|
|Price||Product not available in this region.|
|Alternative name||alpha Synuclein|
|Immunogen||Phosphorylated peptide corresponding to the region including the Tyrosine 125 residue of alpha-Synuclein|
The 140-amino-acid alpha-Synuclein protein is identical to the non-amyloid-beta component precursor (NACP), a presynaptic protein involved in amyloidogenesis in Alzheimer's disease (AD). This protein is expressed in brain, primarily in presynaptic nerve terminals. Although the exact function of the Synucleins has not been determined, they have been linked to the prominent neurodegenerative disorders AD and Parkinson's disease. The Tyrosine 125 (Y125) residue of alpha-Synuclein plays an important role in stress-induced dimerization of the protein and is phosphorylated by Pyk/RAFTK via the Src-family kinases Fyn and c-Src.
The I57-628 antibody recognizes alpha-Synuclein phosphorylated at Y125.
1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
3. Please refer to us for technical protocols.
|Molecular Weight||19 kDa|
Related Products: ABIN967389
|Purification||Purified from tissue culture supernatant or ascites by affinity chromatography.|
|Buffer||Aqueous buffered solution.|
|Preservative||0.09% Sodium azide.|
|Storage||Store undiluted at 4°C.|
|Research Area||Neurology, Alzheimer's Disease|
|Restrictions||For Research Use only|
Ellis, Schwartzberg, Grider et al.: "alpha-synuclein is phosphorylated by members of the Src family of protein-tyrosine kinases." in: The Journal of biological chemistry, Vol. 276, Issue 6, pp. 3879-84, 2001 (PubMed).
Nakamura, Yamashita, Takahashi et al.: "Activated Fyn phosphorylates alpha-synuclein at tyrosine residue 125." in: Biochemical and biophysical research communications, Vol. 280, Issue 4, pp. 1085-92, 2001 (PubMed).
Takahashi, Yamashita, Nakamura et al.: "Tyrosine 125 of alpha-synuclein plays a critical role for dimerization following nitrative stress." in: Brain research, Vol. 938, Issue 1-2, pp. 73-80, 2002 (PubMed).
Nakamura, Yamashita, Nagano et al.: "Activation of Pyk2/RAFTK induces tyrosine phosphorylation of alpha-synuclein via Src-family kinases." in: FEBS letters, Vol. 521, Issue 1-3, pp. 190-4, 2002 (PubMed).
Forman, Trojanowski, Lee: "Neurodegenerative diseases: a decade of discoveries paves the way for therapeutic breakthroughs." in: Nature medicine, Vol. 10, Issue 10, pp. 1055-63, 2004 (PubMed).