Anti-PDK1 (Ser-241), Phosphospecific Antibody

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 is 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.

Our PDK1 (Ser-241) phosphospecific primary antibody from PhosphoSolutions is rabbit polyclonal. It detects human, mouse, and rat PDK1 (Ser-241) and is antigen affinity purified. It is great for use in WB, IHC.

Phospho-PDK1 (Ser-241) synthetic peptide (coupled to carrier protein) corresponds to amino acids surrounding serine 241 in human PDK1. This sequence is highly conserved in rat and mouse PDK1.

For research use only. Not intended for therapeutic or diagnostic use. Use of all products is subject to our terms and conditions, which can be viewed on our website.

The purified antibody detects a 65 kDa* protein corresponding to the apparent molecular mass of PDK1 on SDS-PAGE immunoblots of human MDA-MB-435 cells treated with EGF, but not in untreated cells. PDK1 (Ser-241) reactivity was also observed by immunohistochemistry in human breast carcinoma tissue.