bsm-70329M

DATASHEET

Host: Mouse

Target Protein: Akt (N-terminal region)

Specificity: 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.

Clonality: Monoclonal

Isotype: IgG1

Swiss Prot: P31749

Source: Clone M101 was generated from a recombinant protein containing amino acid residues in the N-terminal region of human Akt1.

Purification: Purified by Protein A.

Storage Buffer: PBS + 1 mg/ml BSA, 0.05% NaN3 and 50% glycerol

Storage: Storage at -20°C is recommended, as aliquots may be taken without freeze/thawing due to presence of 50% glycerol. Stable for at least 1 year at -20°C.

Background:

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 PKCδ and PKCζ. Ceramide-activated PKCζ 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.