IRS-1 (pY896) Mouse, PE, Clone: K9-211, BD

Description

• 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
• Intracellular Staining