The serine-threonine protein kinase encoded by the AKT1 gene is catalytically inactive in serum-starved primary and immortalized fibroblasts. AKT1 and the related AKT2 are activated by platelet-derived growth factor. The activation is rapid and specific, and it is abrogated by mutations in the pleckstrin homology domain of AKT1. It was shown that the activation occurs through phosphatidylinositol 3-kinase. In the developing nervous system AKT is a critical mediator of growth factor-induced neuronal survival. Survival factors can suppress apoptosis in a transcription-independent manner by activating the serine/threonine kinase AKT1, which then phosphorylates and inactivates components of the apoptotic machinery. Mutations in this gene have been associated with the Proteus syndrome. Multiple alternatively spliced transcript variants have been found for this gene.

Phospho-Akt (p-AKT) antibody detects endogenous levels of Akt only when phosphorylated at Ser473.

Reference: http://www.ncbi.nlm.nih.gov/gene/207

Assay type: Immunohistochemistry (IHC)
What is analyzed: Semi-quantitative detection of  human phosphorylated p-AKT
Platform: Manual assay
Kit/antibody: Rabbit monoclonal to p-AKT phosphorylated at serine 473 (3787, Cell Signaling)
Tissue Type: Lung carcinoma
Required material: FFPE tissue