General protein kinase capable of phosphorylating several known proteins. Phosphorylates TBC1D4. Signals downstream of phosphatidylinositol 3-kinase (PI3K) to mediate the effects of various growth factors such as platelet-derived growth factor (PDGF), epidermal growth factor (EGF), insulin and insulin-like growth factor I (IGF-I). Plays a role in glucose transport by mediating insulin-induced translocation of the GLUT4 glucose transporter to the cell surface. Mediates the antiapoptotic effects of IGF-I. Mediates insulin-stimulated protein synthesis by phosphorylating TSC2 at 'Ser-939' and 'Thr-1462', thereby activating mTORC1 signaling and leading to both phosphorylation of 4E-BP1 and in activation of RPS6KB1. Promotes glycogen synthesis by mediating the insulin-induced activation of glycogen synthase. /General protein kinase capable of phosphorylating several known proteins. IGF-1 leads to the activation of AKT3, which may play a role in regulating cell survival. Capable of phosphorylating several known proteins. Truncated isoform 2/PKB gamma 1 without the second serine phosphorylation site could still be stimulated but to a lesser extent.1) Nelms K, et al. (1999) Annu Rev Immunol. 17:701-738. Malabarba M G, et al. (1996) Biochem. J. 319:865-872. Hou J, et al. (1994) Science. 265:1701-1706. Quelle F W, et al. (1995) Mol Cell Biol. 15: 3336-3343. More
AKT1/AKT2/AKT3 (phospho-Tyr315/316/312) antibody was raised against a peptide sequence around phosphorylation site of tyrosine 315/316/312 (P-E-Y (p) -L-A) derived from Human AKT1/AKT2/AKT3.
IFIHCWB
HumanMouseRat
Western blot analysis of lysed extracts from HepG2 cells untreated or treated with EGF using AKT1/AKT2/AKT3 (phospho-Tyr315/316/312).
Top Image: Immunohistochemical analysis of paraffin-embedded human breast carcinoma tissue using AKT1/AKT2/AKT3 (Phospho-Tyr315/316/312). Bottom Image: Immunofluorescence staining of methanol-fixed HeLa cells using AKT1/AKT2/AKT3 (phospho-Tyr315/316/312).
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