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Discover high-quality research tools to investigate GLP-1 mechanisms and next-generation metabolic targets.
OBESITY RESEARCH SOLUTIONSAkt1 and Akt2, also known as protein kinase Bα (PKBα) and PKBβ, respectively, are serine/threonine kinase belonging to the AGC kinase family and two 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 They are comprised 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 and are the primary isoforms in endothelial cells and insulin-responsive tissues, respectively.3 Akt1E17K is an activating mutation that has been found in tumor tissue isolated from patients with breast, colorectal, or ovarian cancer.4 Akt2E17K mutations have been found in patients with hypoglycemia.5 Cayman's Akt1E17K/Akt2E17K Rabbit Monoclonal Antibody (Clone RM336) can be used for ELISA, immunohistochemistry (IHC), and Western blot (WB) applications.
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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. A transforming mutation in the pleckstrin homology domain of AKT1 in cancer. Nature 448(7152), 439-444 (2007).
5. An activating mutation of AKT2 and human hypoglycemia. Science 334(6055), 474 (2011).