Phospho-IRS1 (Tyr989) Blocking Peptide – The purity is >90%,tested by HPLC and MS. Purity

IRS1: an adaptor protein that is one of the major substrates of the insulin receptor kinase. Contains multiple tyrosine phosphorylation motifs that serve as docking sites for SH2-domain-containing proteins including phosphatidylinositol 3-kinase p85 subunit and GRB-2. Phosphorylated on ser/thr residues by kinases including JNK and IKK.

Protein type: Adaptor/scaffold; Motility/polarity/chemotaxis

Chromosomal Location of Human Ortholog: 2q36

Cellular Component: intracellular membrane-bound organelle; cytoplasm; plasma membrane; caveola; nucleus; cytosol

Molecular Function: insulin-like growth factor receptor binding; protein binding; signal transducer activity; protein kinase C binding; phosphoinositide 3-kinase binding; SH2 domain binding; transmembrane receptor protein tyrosine kinase adaptor protein activity; insulin receptor binding

Biological Process: response to peptide hormone stimulus; phosphoinositide 3-kinase cascade; nerve growth factor receptor signaling pathway; positive regulation of glycogen biosynthetic process; negative regulation of insulin receptor signaling pathway; glucose homeostasis; signal transduction; response to insulin stimulus; negative regulation of insulin secretion; positive regulation of glucose import; mammary gland development; positive regulation of mesenchymal cell proliferation; positive regulation of cell proliferation; protein kinase B signaling cascade; epidermal growth factor receptor signaling pathway; fibroblast growth factor receptor signaling pathway; phosphoinositide-mediated signaling; positive regulation of phosphoinositide 3-kinase activity; positive regulation of fatty acid beta-oxidation; cellular response to insulin stimulus; insulin-like growth factor receptor signaling pathway; regulation of gene expression; insulin receptor signaling pathway; innate immune response; positive regulation of insulin receptor signaling pathway; lipid catabolic process; positive regulation of cell migration

Disease: Diabetes Mellitus, Noninsulin-dependent