Protein Kinase B (PKB) is downstream of phosphoinositide 3-kinase (PI3-Kinase) that functions in a critical signaling pathway for receptor-dependent cell activation. PKB activation requires the binding of lipid metabolites phosphatidylinositol 3,4,5-trisphosphate and phosphatidylinositol 3,4-bisphosphate, phospholipid products of PI3-Kinase. These lipids bind to PKB and induce a conformational change in the enzyme, resulting in its translocation to the plasma membrane. Following cell activation, PKB is phosphorylated on Thr-308 by another kinase designated as 3-Phosphoinositide-Dependent Protein Kinase 1 (PDPK1) or also known as PKB Kinase. This kinase probably represents a new family of phospholipid-dependent activities with molecular weights that range from 31 to 220 kDa. PDPK1 consists of 559 amino acids with an N-terminal catalytic domain and a pleckstrin-homology (PH) domain located in the C-terminal region. Like PKB, PDPK1 requires the presence of phosphatidylinositol 3,4,5-trisphosphate for maximal activity. Thus, PDPK1 acts upstream of PKB and may control signals important for proliferation, apoptosis, and metabolism.
This antibody is routinely tested by western blot analysis. Other applications were tested at BD Biosciences Pharmingen during antibody development only or reported in the literature.