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.1) Xing J, et al. (1998) Mol Cell Biol 18 (4): 1946-55. Tan Y, et al. (1996) EMBO J; 15 (17): 4629-42. Hao, M. et al. (1996) J. Biol. Chem. 271, 29380-29385. Mayo LD, et al. (2001) Biol Chem; 276 (27): 25184-9. More
AKT1 (phospho-Thr450) antibody was raised against a peptide sequence around phosphorylation site of threonine 450 (T-I-T (p) -P-P) derived from Human AKT1.
IFIHCWB
HumanMouseRat
Western blot analysis of lysed extracts from 293 cells untreated or treated with EGF using AKT1 (phospho-Thr450).
Top Image: Immunohistochemical analysis of paraffin-embedded human breast carcinoma tissue using AKT1 (Phospho-Thr450). Bottom Image: Immunofluorescence staining of methanol-fixed HeLa cells using AKT1 (phospho-Thr450).
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