3-Phosphoinositide-dependent kinase 1 (PDK1), also known as PKB kinase, was identified as the activator of the survival kinase Akt/PKB. Several important substrates of PDK1 include p70S6 kinase, PKAs, PKCs, SGKs, RSKs, and PAKs. PDK1 is a member of the AGC superfamily of serine/threonine kinases. Through the phosphorylation of downstream kinases, like Akt, PDK1 has been shown to be involved in several different cell functions, such as protein synthesis, cell survival, glucose metabolism, and cell adhesion and migration. The regulation of PDK1 occurs through lipid second messengers and phosphorylation. Multiple serine sites are phosphorylated on PDK1. Serine 241 phosphorylation is required for PDK1 activity, while serine 396 has been implicated in PDK1 nuclear translocation. Tyrosine phosphorylation may also regulate PDK1 activity. Tyrosines 9 and 373/376 are phosphorylated by c-Src in vitro. Tyr-373/Tyr-376 are important for PDK1 activity, while Tyr-9 phosphorylation permits Tyr-373/Tyr-376 phosphorylation by c-Src. In addition, Tyr-9 may be important during angiotensin-II-induced focal adhesion formation.
Clone M146 was generated from a recombinant protein containing amino acid residues in the C-terminal region of human PDK1. This sequence is highly conserved in rat and mouse PDK1
Target:
PDK1 (C-terminal region)
Application Dilute:
WB(1:300-5000)
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