Akt1 PH Domain Rabbit Monoclonal Antibody (Clone RM316)

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 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.³ The Akt PH domain is required for membrane localization and activation of Akt.⁴ It binds PIP₃ and PIP₂ generated by PI3K, which is activated by a variety of growth factors, recruiting Akt to the plasma membrane where it is phosphorylated at threonine 308 and serine 473, resulting in its activation.² A glutamic acid-to-lysine substitution at glutamic acid 17 (E17K) in the Akt1 PH domain leads to constitutive Akt1 membrane localization and activation and has been found in tumors isolated from patients with breast, colorectal, or ovarian cancer.⁵ Cayman's Akt1 PH Domain Rabbit Monoclonal Antibody (Clone RM316) can be used for immunohistochemistry (IHC) and Western blot (WB) applications.

WARNING This product is not for human or veterinary use.

1. Dummler, B., and Hemmings, B.A. Physiological roles of PKB/Akt isoforms in development and disease. Biochem. Soc. Trans. 35(Pt 2), 231-235 (2007).

2. Bellacosa, A., Kumar, C.C., Di Cristofano, A., et al. Activation of AKT kinases in cancer: Implications for therapeutic targeting. Adv. Cancer Res. 94, 29-86 (2005).

3. McKay, J.A., Douglas, J.J., Ross, V.G., et al. Cyclin D1 protein expression and gene polymorphism in colorectal cancer. Int. J. Cancer 88(1), 77-91 (2000).

4. Sun, M., Wang, G., Paciga, J.E., et al. 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).

5. Carpten, J.D., Faber, A.L., Horn, C., et al. A transforming mutation in the pleckstrin homology domain of AKT1 in cancer. Nature 448(7152), 439-444 (2007).