Protein Kinase B (PKB), also known as Rac (Related to the A and C kinases) Protein Kinase, shows 73% and 68% to Protein Kinase C (PKC) and Protein Kinase A (PKA), respectively. It was also identified as the product of the v-akt oncogene from T-cell lymphomas. Akt/PKB mRNA has been reported to be expressed in a wide variety of cell lines and has been detected in porcine brain, heart, liver, kidney, muscle, and ovary. Rac phosphorylates a number of physiological substrates including MBP, glycogen synthetase, PKA RII subunit, and histone H1. Akt/PKB is activated in response to growth factors through the activation of PI3-kinase and Ras. Activation of PI3-Kinase generates phosphatidylinositol 3,4-bisphosphate which may induce the membrane translocation of Akt/PKB coincident with its phosphorylation and activation. Cellular stress leading to the activation of the p38 MAP kinase also induces Akt/PKB activation, indicating a multiplicity of signaling pathways that activate Akt/PKB. Upon activation, Akt/PKB associates with some members of the PKC family of kinases, such as PKCδ and PKCζ. Downstream of Akt/PKB, GSK3 is thus far the only identified substrate for Akt/PKB phosphorylated in vivo.
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.