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 (pSer473) recognises PKB phosphorylated at serine 473 (56 kDa).
Synthetic phosphorylated peptide corresponding to (pSer473) PKBα (human, amino acids 461-477 with N-terminally added lysine), conjugated to KLH. The sequence is identical in rat, mouse, viral Akt and bovine PKBα and is highly conserved in chicken PKBα-(single amino acid substitution). The immunogen sequence is conversed to a lesser degree in PKBγ (88%) and PKBβ (64%).
Anti-phospho-PKB (pSer473) antibody produced in rabbit has been used in western blotting.
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
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