PIK3CA Protein, Human (sf9, His, StrepⅡ)

PI3-Kinase p110α is a phosphoinositide-3-kinase (PI3K) that phosphorylates phosphatidylinositol (PI) and its phosphorylated derivatives at position 3 of the inositol ring to produce 3-phosphoinositides. It utilizes ATP and PtdIns(4,5)P2 (phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 recruits PH domain-containing proteins such as AKT1 and PDPK1 to the membrane, activating signaling cascades involved in cell growth, survival, proliferation, motility, and morphology. This kinase participates in cellular signaling in response to various growth factors and is involved in AKT1 activation upon stimulation by receptor tyrosine kinase ligands like EGF, insulin, IGF1, VEGFA, and PDGF. It also plays a role in signaling via insulin-receptor substrate (IRS) proteins and is essential for endothelial cell migration during vascular development through VEGFA signaling, potentially by regulating RhoA activity. Additionally, it is required for lymphatic vasculature development, possibly by binding to RAS and activation by EGF and FGF2 (but not PDGF), and regulates invadopodia formation via the PDPK1-AKT1 pathway. In embryonic stem cells, it contributes to cardiomyogenesis through an AKT1 pathway and vasculogenesis via PDK1 and protein kinase C pathways. Beyond its lipid kinase activity, it exhibits serine-protein kinase activity, leading to autophosphorylation of the p85α regulatory subunit and phosphorylation of other proteins, including 4EBP1, H-Ras, and the IL-3 beta c receptor. By similarity: It plays a role in the positive regulation of phagocytosis and pinocytosis.