Anti-phospho-AKT1 Antibody, Thr479 from rabbit, purified by affinity chromatography

RAC-alpha serine/threonine-protein kinase (UniProt: P31749; EC: 2.7.11.1; Protein kinase B, PKB, Protein kinase B alpha, PKB alpha, Proto-oncogene c-Akt, RAC-PK-alpha, AKT1) is encoded by the AKT1 (also known as PKB, RAC) gene (Gene ID: 207) in human. AKT1 is one of 3 closely related serine/threonine-protein kinases (AKT1, AKT2 and AKT3) that regulate many processes including metabolism, proliferation, cell survival, growth and angiogenesis. In mammals these 3 isoforms of AKT exhibit a high degree of homology, but differ slightly in the localization of their regulatory phosphorylation sites. AKT1 is constitutively phosphorylated on Ser124, in the region between PH and catalytic domains, and on Thr450, in the C-terminal region in unstimulated cells. Phosphorylation at Thr308 and Ser473 induces complete activation of AKT1. AKT1 contains one PH domain (aa 5-108), one protein kinase domain (aa 150-408), and one AGC-kinase C-terminal domain (aa 409-480). Binding of the PH domain to phosphatidylinositol 3,4,5-trisphosphate (PIP3) results in its targeting to the plasma membrane. AKT1 can be phosphorylated at Ser477/Thr479 by Cdk2/Cyclin A, which locks it into an active conformation. Ser477/Thr479 phosphorylation is believe to trigger Akt1 activation either through enhancing the association between AKT1 and mTORC2 to promote phosphorylation of Ser473, or by functionally compensating for phosphorylated Ser473 to lock AKT1 in its active conformation. AKT1 phosphorylated at Ser477/Thr479 is reported to display increased association with Sin1 and mTOR complexes. (Ref.: Liu, P et al (2014). Nature. 508(7497): 541-545).