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Akt, also known as protein kinase B (PKB), is a serine/threonine kinase belonging to the AGC kinase family and has three isoforms in mammals: Akt1, Akt2, and Akt3.1,2 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 Akt 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. Akt1 and Akt2 are ubiquitously expressed whereas Akt3 is primarily expressed in the placenta, ovary, and spleen, and each isoform shows distinct subcellular localizations: Akt1 in the cytoplasm, Akt2 in the mitochondria, and Akt3 in the nucleus and nuclear membrane.3,4 Akt is activated following phosphorylation at threonine 308, 309, and 305 and serine 473, 474, and 472 for Akt1, -2, and -3, respectively.4 Hyperactivation of Akt via mutations, amplification, or overexpression is associated with various cancers.2 Cayman’s Akt (Phospho-Ser473) Rabbit Monoclonal Antibody (Clone RM251) can be used for immunohistochemistry (IHC) and Western blot (WB) applications. The antibody recognizes Akt (phospho-Ser473) at 56 kDa from human, mouse, rat, and bovine samples.
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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. Molecular cloning, expression and characterization of the human serine/threonine kinase Akt-
4. The Akt isoforms are present at distinct subcellular locations. Am. J. Physiol. Cell Physiol. 298(3), C580-C591 (2010).