Recombinant PDPK1 protein (His tag)

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Recombinant Human 3-phosphoinositide-dependent protein kinase 1 (hPDK1) fragment (residues 75-359) - a highly purified protein containing the complete catalytic kinase domain. This fragment serves as an essential tool for studying the master regulatory functions of PDK1 in cellular signaling pathways, particularly its role in phosphorylating and activating key AGC family kinases.

3-phosphoinositide-dependent protein kinase 1 (PDK1) is a crucial serine/threonine kinase that functions as a master regulator in cellular signaling. It phosphorylates and activates multiple members of the AGC kinase family, including protein kinase B (PKB/AKT), p70 and p90 ribosomal S6 kinases, protein kinase C isoforms, serum and glucocorticoid-inducible kinases, and p21-activated kinase-1. PDK1 plays a central role in insulin signaling by providing the activating phosphorylation to PKB/AKT1, thereby regulating downstream targets controlling cell proliferation, survival, glucose uptake, and amino acid storage. The protein exhibits complex subcellular localization, being found in the cytoplasm, nucleus, cell membrane, and focal adhesions, with its localization influenced by factors such as insulin stimulation, tyrosine phosphorylation, and association with binding partners like GRB14 and INSR. PDK1 also participates in TGF-beta signaling regulation, NF-kappa-B pathway activation through IKKB phosphorylation, and various developmental processes across different cell types.