A phospho specific peptide corresponding to residues surrounding Threonine 308 of human Akt1 was used as immunogen. The antibody detects Akt1 phosphorylated at Threonine 308.
Buffer
50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.
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. Multiple alternatively spliced transcript variants have been found for this gene. [provided by RefSeq].
Related Pathway
Apoptosis
Delta-Notch Signaling Pathway
EGFR1 Signaling Pathway
Focal Adhesion
Hemostasis
Jak-STAT signaling pathway
MAPK signaling pathway
Signaling by GPCR
Toll-like receptor signaling pathway
Wnt Signaling Pathway
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Western blot analysis on NIH 3T3 cell lysates using anti-Phospho-Akt1 (pT308) RabMAb (TA303391), 1:10,000 dilution. Cells were either (A) untreated (B) treated with PDGF </div>
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