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Akt1, also known as protein kinase Bα (PKBα), is a serine/threonine kinase belonging to the AGC kinase family and one of three Akt isoforms in mammals.1,2 Akt kinases function downstream of activated tyrosine kinases and PI3K to regulate a variety of cellular processes, including cell size, growth, proliferation, and survival, as well as genome stability, glucose metabolism, and neovascularization.2 Akt1, like Akt2 and Akt3, is composed of an N-terminal pleckstrin homology (PH) domain, which binds to phosphatidylinositol-(3,4,5)-triphosphate (PIP3) and phosphatidylinositol-(3,4)-diphosphate (PIP2), a kinase domain, and a C-terminal regulatory hydrophobic motif. It is ubiquitously expressed and is the primary isoform in endothelial cells.3 Akt1 is activated via recruitment to the plasma membrane, which is mediated by the interaction of the Akt1 PH domain with PI3K-generated PIP3 and PIP2, and subsequent phosphorylation at threonine 308 and serine 473.2 Increased Akt1 kinase activity has been found in tumor tissue isolated from patients with prostate, breast, and ovarian cancers.4 Cayman’s Akt1 (human, recombinant) protein was phosphorylated by recombinant 3-phosphoinositide-dependent kinase 1 (PDK1) and can be used for enzyme activity assays.
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1. Physiological roles of PKB/Akt isoforms in development and disease. Biochem. Soc. Trans. 35(Pt 2), 231-235 (2007).
2. Activation of AKT kinases in cancer: Implications for therapeutic targeting. Adv. Cancer Res. 94, 29-86 (2005).
3. AKT/PKB signaling: Navigating downstream. Cell 129(7), 1261-1274 (2007).
4. AKT1/PKBα kinase is frequently elevated in human cancers and its constitutive activation is required for oncogenic transformation in NIH3T3 cells. Am. J. Pathol. 159(2), 431-437 (2001).