Protein kinase B (PKB, also known as Akt) is a serine/threonine protein kinase and a key regulator of signal transduction processes. Important processes such as cell cycle, proliferation and apoptosis are regulated by PKB in response to stimuli such as growth factors, insulin and cytokines. Three isoforms of PKB have been identified, α, β and γ. PKB α is reportedly overexpressed in breast cancer cell lines, whereas PKB β is overexpressed in ovarian and pancreatic cancers. On cell stimulation by growth factors or insulin, PKB α translocates to the cell membrane, where it undergoes full activation by phosphorylation at Thr308 and Ser 473, by PDK1 and PDK2. PKB α plays a crucial role in several downstream pathways involved in glycogen synthesis, protein translation and cell proliferation. PKB is also a potent inhibitor of apoptotic cell death by suppressing BAD-induced death
Anti-phospho PKB (pThr308) recognises PKB phosphorylated at threonine 308 (56 kDa).
synthetic phosphopeptide corresponding to the pThr308 region of human PKBα (amino acids 301-315).
Anti-phospho PKB (pThr308) may be used for detection and localization of phospho-PKB by immunoblotting. A minimum dilution of 1:1000 may be used for detection by immunoblotting in PDGF-treated mouse NIH3T3 cells and peroxide-treated Rat-1 fibroblast cell line.
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
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