Synuclein, alpha (Non A4 Component of Amyloid Precursor) (SNCA) (Tyr125) antibody

Antigen: Synuclein, alpha (Non A4 Component of Amyloid Precursor) (SNCA)

Binding Site: Tyr125

Clonality: Monoclonal (I57-628)

Host: Mouse

Reactivity: Human

Conjugate: Un-conjugated

Application: Western Blotting (WB)

Catalog no.: ABIN967584

Additional Information

Alternative name: alpha Synuclein

Immunogen: Phosphorylated peptide corresponding to the region including the Tyrosine 125 residue of alpha-Synuclein

Format: Liquid

Isotype: IgG2b, kappa

Clone: I57-628

Description: 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.

Characteristics: 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

Comments:

Related Products: ABIN967389

Application Details

Concentration: 0.5 mg/ml

Purity: Purified

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

Images

Western blot analysis of alpha-Synuclein (pY125). Lysates from control (first panel) and pervanadate-treated (second panel) HEK 293 cells were probed with mAb I57-628 at concentrations of 0.002, 0.001, and 0.0005 µg/ml (Lanes 1, 2, and 3, respectively). alpha-Synuclein (pY125) is identified as a strong band of 19 kDa in the pervanadate-treated cells.

Publications

Product: 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).