Cd220 Mouse, Unlabeled, Clone: 46, Bd, Mouse Monoclonal Antibody, Each

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Insulin receptor (ir) is a transmembrane receptor tyrosine kinase which, upon insulin binding, initiates a cascade of events, including autophosphorylation, phosphorylation of cellular protein substrates, glucose transport, and glycogen synthesis. Ir is synthesized as a large glycosylated precursor that is cleaved upon maturation into a 130kda α-subunit with kinase activity and a 95kda β-subunit. The active insulin receptor is a heterotetramer of homologus α and β subunits joined by disulfide bonds. Among the major cytosolic substrates of the insulin receptor are irs-1 and -2, β-adrenergic receptor, and pp15 (adipocyte lipid-binding protein, albp). Autophosphorylation of the ir recruits irs-1 and -2 to the phosphotyrosines. Subsequently, the phosphorylated irs-1 and -2 act as docking sites for other signaling proteins like pi3-kinase, shc, ptp1d, nck, etc. In addition, the phosphatase lar is tightly associated with the ir and lar becomes activated after insulin stimulation dephosphorylating the ir and its substrates. Therefore, lar provides a turn-off mechanism in insulin signaling.Host species: mouseclone: 46isotype: igg1species reactivity: mouseimmunogen: human insulin pro-receptor β subunit 1006-1144formula weight [chemical]: 95kdaimmunofluorescence, immunoprecipitation, western blotting