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Western blot analysis of PDPK1 (pS241) in human T lymphocytes. Lysates from calyculin A- plus okadaic acid -treated Jurkat cells were probed with purified mouse anti-PDPK1 (pS241) at concentrations of 0.5 (lanes 1 and 4), 0.25 (lanes 2 and 5), and 0.125 µg/ml (lanes 3 and 6) with (lanes 1-3) or without (lanes 4-6) lambda protein phosphatase treatment. PDPK1 (pS241) is identified as a strong band of 63 kDa in the lysate without phosphatase treatment.
BD Pharmingen™ Purified Mouse anti-PDPK1 (pS241)
Regulatory Status Legend
Any use of products other than the permitted use without the express written authorization of Becton, Dickinson and Company is strictly prohibited.
Preparation And Storage
Product Notices
- Since applications vary, each investigator should titrate the reagent to obtain optimal results.
- Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
- Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
The serine/threonine kinase 3-Phosphoinositide-Dependent Protein Kinase-1 (PDPK1, also known as PDK1) contributes to the activation of many important kinases in the insulin and IGF-1 signaling pathways. It acts downstream of phosphatidylinositol 3-kinase (PI3-kinase) to phosphorylate residues in the activation loops of many cellular kinases, including protein kinase B (PKB/Akt), PKC isoforms, p70 S6 kinase, and PDPK1 itself. The autophosphorylation of PDPK1 at serine 241 (S241) has recently been suggested to play a role in the regulation of PDPK1. It has been proposed that PDPK1 activity plays a key role in the regulation of various cellular events such as cell proliferation, differentiation, and apoptosis.
The J666-653.44.22 monoclonal antibody recognizes the phosphorylated S241 in the activation loop of human PDPK1. The orthologous phosphorylation site in mouse and rat PDPK1 is S244.
Development References (2)
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Komander D, Kular G, Deak M, Alessi DR, van Aalten DM. Role of T-loop phosphorylation in PDK1 activation, stability, and substrate binding. J Biol Chem. 2005; 280(19):18797-18802. (Biology). View Reference
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Wick MJ, Ramos FJ, Chen H, et al. Mouse 3-phosphoinositide-dependent protein kinase-1 undergoes dimerization and trans-phosphorylation in the activation loop. J Biol Chem. 2003; 278(44):42913-42919. (Biology). View Reference
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