The 3-phosphoinositide-dependent protein kinase-1 (PDK1, PKB kinase), is a master regulator of AGC kinases. It mediates cellular effects by activating major pathways involving PKB/Akt , S6K, RSK, SGK and the PKC isoforms. PDK1 is ubiquitously present in cells and is constitutively active. PDK1 is a critical activator of PKB/Akt as it mediates phosphorylation at Thr308 in the catalytic domain, thus plays a significant role on oncogenic signalling by PI3K, cell growth, survival, proliferation and migration. By regulating AGC kinases PDK1 is actively involved in the regulation of protein translation and metabolism, and serum and gluco-corticoid induced signalling. Anti-PDK1 recognizes human PDK1 (60 kDa).
Immunogen
synthetic peptide corresponding to the C-terminus of human PDK1 (amino acids 538-556).
Application
Anti-PDK-1 may be used for detection by immunoblotting at a working dilution of 1:1000. The antibody is suitable for protein microarray.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
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The 3-phosphoinositide-dependent protein kinase-1 (PDK1) mediates the cellular effect of insulin and growth factors by activating a group of kinases including PKB/Akt, S6K, RSK, SGK and PKC isoforms. PDK1 possesses two regulatory domains namely a Pleckstrin Homology (PH) domain that
Current topics in microbiology and immunology, 346, 9-29 (2010-06-22)
Most of the cellular responses to phosphatidylinositol 3-kinase activation and phosphatidylinositol 3,4,5-trisphosphate production are mediated by the activation of a group of AGC kinases comprising PKB, S6K, RSK, SGK and PKC isoforms, which play essential roles in regulating physiological processes
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