AKT3, clone 9A5.H9.G7

This primary and secondary antibody pair has been carefully chosen to give best resutls. Anti-AKT3 antibody is directed against human AKT3. The antibody detects both unphosphorylated and phosphorylated forms of the protein. Anti-AKT3 antibody was purified from ascites by Protein A chromatography. Cross reactivity with AKT3 from other species has not been determined, however, the sequence of the immunogen shows 100% identity to human, mouse, and rat, therefore, cross reactivity is expected. Cross-reactivity with AKT2 and AKT1 has not been determined. HRP secondary antibody was prepared from monospecific antiserum by immunoaffinity chromatography using Mouse IgG coupled to agarose beads followed by solid phase adsorption(s) to remove any unwanted reactivities. This product shows balanced reactivity to Mouse IgG1, IgG2a, IgG2b and IgG3 proteins and is suitable to screen IgG class hybridoma clones. Minimal cross reactivity is observed against other Mouse immunoglobulin classes or light chain proteins. This antibody pair is sufficient for up to 5 mini blots at 7.5 x 8 cm2 (1,800 cm2). Protein function: AKT3 is one of 3 closely related serine/threonine- protein kinases (AKT1, AKT2 and AKT3) called the AKT kinase, and which regulate many processes including metabolism, proliferation, cell survival, growth and angiogenesis. This is mediated through serine and/or threonine phosphorylation of a range of downstream substrates. Over 100 substrate candidates have been reported so far, but for most of them, no isoform specificity has been reported. AKT3 is the least studied AKT isoform. It plays an important role in brain development and is crucial for the viability of malignant glioma cells. AKT3 isoform may also be the key molecule in up-regulation and down-regulation of MMP13 via IL13. Required for the coordination of mitochondrial biogenesis with growth factor-induced increases in cellular energy demands. Down-regulation by RNA interference reduces the expression of the phosphorylated form of BAD, resulting in the induction of caspase- dependent apoptosis. [The UniProt Consortium]