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      Purified Mouse anti-α-Synuclein (pY125)
      Purified Mouse anti-α-Synuclein (pY125)
      Western blot analysis of α-Synuclein (pY125).  Lysates from control (left panel) and pervanadate-treated (right 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).  α-Synuclein (pY125) is identified as a strong band of 19 kDa in the pervanadate-treated cells.
      Purified Mouse anti-α-Synuclein (pY125)
      Western blot analysis of α-Synuclein (pY125).  Lysates from control (left panel) and pervanadate-treated (right 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).  α-Synuclein (pY125) is identified as a strong band of 19 kDa in the pervanadate-treated cells.
      Product Details
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      BD Pharmingen™
      Human (QC Testing)
      Mouse IgG2b, κ
      Phosphorylated peptide corresponding to the region including the Tyrosine 125 residue of α-Synuclein
      Western blot (Routinely Tested)
      19 kDa
      0.5 mg/ml
      AB_647301
      Aqueous buffered solution containing ≤0.09% sodium azide.
      RUO


      Preparation And Storage

      Store undiluted at 4°C. The monoclonal antibody was purified from tissue culture supernatant or ascites by affinity chromatography.
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      Recommended Assay Procedures

      Western blot:  Please refer to http://www.bdbiosciences.com/pharmingen/protocols/Western_Blotting.shtml

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      Product Notices

      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 www.bdbiosciences.com/us/s/resources for technical protocols.
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      558246 Rev. 3
      Antibody Details
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      I57-628

      The 140-amino-acid α-Synuclein protein is identical to the non-amyloid-β 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 α-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 α-Synuclein phosphorylated at Y125.

      558246 Rev. 3
      Format Details
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      Purified
      Tissue culture supernatant is purified by either protein A/G or affinity purification methods. Both methods yield antibody in solution that is free of most other soluble proteins, lipids, etc. This format provides pure antibody that is suitable for a number of downstream applications including: secondary labeling for flow cytometry or microscopy, ELISA, Western blot, etc.
      Purified
      558246 Rev.3
      Citations & References
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      Development References (5)

      1. Ellis CE, Schwartzberg PL, Grider TL, Fink DW, Nussbaum RL. α-Synuclein is phosphorylated by members of the Src family of protein-tyrosine kinases. J Biol Chem. 2001; 276(6):3879-3884. (Biology).
      2. Forman MS, Trojanowski JQ, Lee VM-Y. Neurodegenerative diseases: a decade of discoveries paves the way for therapeutic breakthroughs. Nat Med. 2004; 10(10):1055-1063. (Biology).
      3. Nakamura T, Yamashita H, Nagano Y, et al. Activation of Pyk2/RAFTK induces tyrosine phosphorylation of α-synuclein via Src-family kinases. FEBS Lett. 2002; 521(1 - 3):190-194. (Biology).
      4. Nakamura T, Yamashita H, Takahashi T, Nakamura S. Activated Fyn phosphorylates alpha-synuclein at tyrosine residue 125. Biochem Biophys Res Commun. 2001; 280(4):1085-1092. (Biology).
      5. Takahashi T, Yamashita H, Nakamura T, Nagano Y, Nakamura S. Tyrosine 125 of alpha-synuclein plays a critical role for dimerization following nitrative stress. Brain Res. 2002; 938(1 - 2):73-80. (Biology).
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      558246 Rev. 3

      Please refer to Support Documents for Quality Certificates


      Global - Refer to manufacturer's instructions for use and related User Manuals and Technical data sheets before using this products as described


      Comparisons, where applicable, are made against older BD Technology, manual methods or are general performance claims.  Comparisons are not made against non-BD technologies, unless otherwise noted.

      For Research Use Only. Not for use in diagnostic or therapeutic procedures.

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