Binds to activated (phosphorylated) protein-Tyr kinases, through its SH2 domain, and acts as an adapter, mediating the association of the p110 catalytic unit to the plasma membrane. Necessary for the insulin-stimulated increase in glucose uptake and glycogen synthesis in insulin-sensitive tissues. Binds to activated (phosphorylated) protein-tyrosine kinases through its SH2 domain and regulates their kinase activity. During insulin stimulation, it also binds to IRS-1./Binds to activated (phosphorylated) protein-tyrosine kinases, through its SH2 domain, and acts as an adapter, mediating the association of the p110 catalytic unit to the plasma membrane.1) Stoyanov, B. et al. (1995) Science 269, 690-3. Simpson, L. and Parsons, R. (2001) Exp Cell Res 264, 29-41. Neri, L. M. et al. (2002) Biochim Biophys Acta 1584, 73-80.
Immunogen
PI3K P85 (phospho-Tyr467) antibody was raised against a peptide sequence around phosphorylation site of tyrosine 467 (L-Y (p) -E-E-Y) derived from Human PI3K P85.