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Description
Protein Kinase B (PKB) is downstream of phosphoinositide 3-kinase (PI3-Kinase) that functions in a critical signaling pathway for receptor-dependent cell activation. PKB activation requires the binding of lipid metabolites phosphatidylinositol 3,4,5-trisphosphate and phosphatidylinositol 3,4-bisphosphate, phospholipid products of PI3-Kinase. These lipids bind to PKB and induce a conformational change in the enzyme, resulting in its translocation to the plasma membrane. Following cell activation, PKB is phosphorylated on Thr-308 by another kinase designated as 3-Phosphoinositide-Dependent Protein Kinase 1 (PDPK1) or also known as PKB Kinase. This kinase probably represents a new family of phospholipid-dependent activities with molecular weights that range from 31 to 220kDa. PDPK1 consists of 559 amino acids with an N-terminal catalytic domain and a pleckstrin-homology (PH) domain located in the C-terminal region. Like PKB, PDPK1 requires the presence of phosphatidylinositol 3,4,5-trisphosphate for maximal activity. Thus, PDPK1 acts upstream of PKB and may control signals important for proliferation, apoptosis, and metabolism.
Immunofluorescence, Western Blotting
Specifications
Specifications
| Antigen | PDPK1 |
| Applications | Western Blot |
| Classification | Monoclonal |
| Clone | 5 |
| Concentration | 250μg/mL |
| Conjugate | Unconjugated |
| Description | PKB Kinase, Akt Kinase, PDK1 |
| Formulation | Aqueous buffered solution containing BSA, glycerol, and ≤0.09% sodium azide. |
| Host Species | Mouse |
| Immunogen | Rat PDPK1 aa. 439-555 |
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