BD, 558378, Purified Mouse anti-IRS-1 (pY896) K9-211.52.30

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.

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