| Overview |
| bsm-70329m |
| Akt (N-terminal region) Antibody |
| WB |
| The antibody detects a 60 kDa* protein corresponding to the apparent molecular mass of phoshorylated Akt on SDS-PAGE immunoblots of A431 + calyculin A cell lysate. Similar results were seen in calyculin A treated human aortic endothelial and HeLa cells, rabbit spleen fibroblasts, and rat pituitary cells. This sequence is highly conserved in human and mouse Akt, and may recognize Akt2 and Akt3. |
| Human, Mouse, Rat |
| Specifications |
| Unconjugated |
| Mouse |
| Clone M101 was generated from a recombinant protein containing amino acid residues in the N-terminal region of human Akt1. |
| Monoclonal |
| M101 |
| IgG1 |
| Purified by Protein A. |
| PBS + 1 mg/ml BSA, 0.05% NaN3 and 50% glycerol |
| Storage at -20C is recommended, as aliquots may be taken without freeze/thawing due to presence of 50% glycerol. Stable for at least 1 year at -20C. |
| Target |
| P31749 |
| PKBalpha, PKB, AKT |
| Akt (PKB, Rac kinase) is a 60kDa ser/thr kinase critical for controlling diverse cellular functions, including glucose metabolism, gene transcription, cell proliferation, and apoptosis. Akt phosphorylates a number of substrates including MBP, glycogen synthetase, PKA RII subunit, and histone H1. Akt is activated in response to insulin and growth factors in a PI3-kinase dependent manner. Activation of PI3-Kinase generates phosphatidylinositol 3,4-bisphosphate, which induces membrane translocation of Akt coincident with its phosphorylation at Thr-308 and Ser-473. Upon activation, Akt associates with members of the PKC family of kinases, such as PKC_ and PKC_. Ceramide-activated PKC_ leads to phosphorylation of Thr-34 within the pleckstrin homology domain of Akt. This phosphorylation inhibits PIP3 binding to Akt preventing activation of the kinase and may lead to cermide-induced cell death. |
| Application Dilution |
| WB |
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