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Phosphoinositide-dependent protein kinase-1 (PDK1) activator (Kd = 10.3 μM). Binds exclusively to the PIF-binding pocket of PDK1, distinct from the ATP binding site.
|Storage||Store at +4°C|
The technical data provided above is for guidance only. For batch specific data refer to the Certificate of Analysis.
Tocris products are intended for laboratory research use only, unless stated otherwise.
References are publications that support the biological activity of the product.
Hindie et al (2009) Structure and allosteric effects of low-molecular-weight activators on the protein kinase PDK1. Nat.Chem.Biol. 5 758 PMID: 19718043
Stroba et al (2009) 3,5-diphenylpent-2-enoic acids as allosteric activators of the protein kinase PDK1: structure-activity relationships and thermodynamic characterization of binding as paradigms for PIF-binding pocket-targeting compounds. J.Med.Chem. 52 4683 PMID: 19606904
Williams (2010) Elastic network model of allosteric regulation in protein kinase PDK1. BMC Struct.Biol. 10 11 PMID: 20500829
Zhu et al (2010) Reprogramming of human primary somatic cells by OCT4 and chemical compounds. Cell Stem Cell. 7 651 PMID: 21112560
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Keywords: PS 48, PS 48 supplier, phosphoinositide-dependent, protein, kinase, 1, pdk1, activators, allosteric, PS48, Phosphoinositide-dependent, Kinase, PDK1, Enzyme, Substrates, /, Activators, 4087, Tocris Bioscience
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