PDK1 (human, recombinant)

PDK1 (human, recombinant)

CAT N°: 37315
Price:

542.00 460.70

3-Phosphoinositide-dependent protein kinase 1 (PDK1) is a serine/threonine kinase with roles in cell survival, differentiation, and proliferation, metabolic regulation, and immune development.{65465,65466,65467} It is composed of an N-terminal bilobular kinase domain, with the small lobe housing a PIF-pocket/?C-helix region and the large lobe containing an activation loop, and a C-terminal PH domain.{65465} PDK1 is activated by autophosphorylation of serine 241 in the activation loop, a residue that is poorly accessible to phosphatases, and is considered constitutively active.{65465} It phosphorylates and activates various members of the AGC protein kinase family, including Akt, p70 ribosomal S6 kinase (p70S6K), serum/glucocorticoid regulated kinase (SGK), and PKC to regulate the PI3K/Akt, Ras/MAPK, and Myc signaling pathways.{65465,65466} Gene amplification of PDPK1, the gene encoding PDK1, is associated with poor prognosis in patients with breast cancer and metastasis in patients with prostate cancer.{65465} Knockdown of Pdpk1 promotes axon regeneration in a mouse model of sciatic nerve injury and inhibits T follicular helper (Tfh) cell differentiation and germinal center responses in a mouse model of acute lymphocytic choriomeningitis virus (LCMV) infection.{65466,65467} Cayman’s PDK1 (human, recombinant) protein is expressed with an N-terminal His-TEV tag, which is removed during the protein purification process, leaving behind an N-terminal glycine residue on the full-length protein. This protein can be used for the phosphorylation of other proteins, such as Akt, and Western blot (WB).

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