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      Purified Mouse anti-IRS-1 (pY896)
      Purified Mouse anti-IRS-1 (pY896)
      Western blot analysis of IRS-1 (pY896) in transformed human epithelial cells.  Lysates from control (lanes 1-3) and IGF-I-treated (Cat. No. 354037, lanes 4-6) 293 fetal kidney cell line were probed with purified mouse anti-IRS-1 (pY896) monoclonal antibody at concentrations of 0.064 (lanes 1 and 4), 0.032 (lanes 2 and 5), and 0.016 µg/ml (lanes 3 and 6).  IRS-1 (pY896) is identified as a band of 160-185 kDa in the treated cells.
      Purified Mouse anti-IRS-1 (pY896)
      Western blot analysis of IRS-1 (pY896) in transformed human epithelial cells.  Lysates from control (lanes 1-3) and IGF-I-treated (Cat. No. 354037, lanes 4-6) 293 fetal kidney cell line were probed with purified mouse anti-IRS-1 (pY896) monoclonal antibody at concentrations of 0.064 (lanes 1 and 4), 0.032 (lanes 2 and 5), and 0.016 µg/ml (lanes 3 and 6).  IRS-1 (pY896) is identified as a band of 160-185 kDa in the treated cells.
      Product Details
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      BD Pharmingen™
      Human (QC Testing)
      Mouse BALB/c IgG2a, κ
      Phosphorylated Human IRS-1 Peptide
      Western blot (Routinely Tested)
      160-185 kDa
      0.5 mg/ml
      AB_647280
      Aqueous buffered solution containing ≤0.09% sodium azide.
      RUO


      Preparation And Storage

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

      1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
      2. Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
      3. 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.
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      558378 Rev. 2
      Antibody Details
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      K9-211

      The IRS (Insulin Receptor Substrate) proteins IRS-1, IRS-2, IRS-3, and IRS-4 are major substrates of the insulin receptor and the insulin-like growth factor-1 (IGF-1) receptor tyrosine kinases.  IRS proteins contain an N-terminal pleckstrin homology (PH) domain, a phosphotyrosine-binding (PTB) domain, and multiple tyrosine phosphorylation sites in the C-terminus.  The IRS-1 protein is widely expressed and, along with IRS-2, mediates somatic growth and carbohydrate metabolic responses to insulin.  Following insulin receptor ligation, IRS-1 binds to the juxtamembrane region of the receptor via the PH and PTB domains and is tyrosine phosphorylated, which facilitates its interaction with SH2 domain-containing signaling proteins.  Specifically, the phosphorylated tyrosine 896 (pY896) of human IRS-1 is a major binding site for the GRB2 (Growth-factor Receptor-Bound protein 2) adaptor protein.  After IRS-1 activation, negative and positive feedback regulates dephosphorylation of its tyrosine sites, which ultimately regulates the magnitude and/or duration of the downstream pleiotropic responses to insulin and IGF-1.

      The K9-211 monoclonal antibody recognizes pY896 of human IRS-1.  The orthologous phosphorylation sites of mouse and rat IRS-1 are Y891 and Y895, respectively.

      558378 Rev. 2
      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
      558378 Rev.2
      Citations & References
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      Development References (5)

      1. Burks DJ, White MF. IRS proteins and β-cell function. Diabetes. 2001; 50(S1):S140-S145. (Biology). View Reference
      2. Gual P, Le Marchand-Brustel Y, Tanti JF. Positive and negative regulation of insulin signaling through IRS-1 phosphorylation. Biochimie. 2005; 87:99-109. (Biology). View Reference
      3. Paz K, Liu YF, Shorer H, et al. Phosphorylation of insulin receptor substrate-1 (IRS-1) by protein kinase B positively regulates IRS-1 function. J Biol Chem. 1999; 274(40):28816-28822. (Biology). View Reference
      4. Ward CW, Gough KH, Rashke M, Wan SS, Tribbick G, Wang J. Systematic mapping of potential binding sites for Shc and Grb2 SH2 domains on insulin receptor substrate-1 and the receptors for insulin, epidermal growth factor, platelet-derived growth factor, and fibroblast growth factor. J Biol Chem. 1996; 271(10):5603-5609. (Biology).
      5. White MF. IRS proteins and the common path to diabetes. Am J Physiol Endocrinol Metab. 2002; 283:E413-E422. (Biology). View Reference
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      558378 Rev. 2

      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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