Product Pathways - PI3K / Akt Signaling
Phospho-SGK3 (Thr320) (D30E6) Rabbit mAb #5642
|W||H (M) (R) (Mk)||Transfected Only||62||Rabbit IgG|
Reactivity Key: H=Human M=Mouse R=Rat Mk=Monkey
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.
Specificity / Sensitivity
Phospho-SGK3 (Thr320) (D30E6) Rabbit mAb detects overexpressed levels of SGK3 protein only when phosphorylated at Thr320.
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Thr320 of human SGK3 protein.
Western blot analysis of extracts from COS-7 cells, untransfected or transfected with human SGK3, and untreated or treated with calf intestinal phosphatase (CIP), using Phospho-SGK3 (Thr320) (D30E6) Rabbit mAb (upper) or SGK3 Antibody #4227 (lower).
Serum and glucocorticoid-inducible kinase (SGK) is a serine/threonine kinase closely related to Akt (1). SGK is rapidly induced in response to a variety of stimuli, including serum, glucocorticoid, follicle stimulating hormone, osmotic shock, and mineralocorticoids. SGK activation can be accomplished via HGF PI3K-dependent pathways and by integrin-mediated PI3K-independent pathways (2,3). Induction and activation of SGK has been implicated in activating the modulation of anti-apoptotic and cell cycle regulation (4-6). SGK also plays an important role in activating certain potassium, sodium, and chloride channels, suggesting its involvement in the regulation of processes such as cell survival, neuronal excitability, and renal sodium excretion (2). SGK is negatively regulated by ubiquitination and proteasome degradation (7).
SGK3 has been shown to be a downstream signaling molecule in the PI3K pathway. Its activation and phosphorylation at Thr320 by PDK1 may be an Akt-independent manner of signaling in cancer (8).
- Webster, M.K. et al. (1993) Mol Cell Biol 13, 2031-40.
- Kobayashi, T. and Cohen, P. (1999) Biochem J 339 ( Pt 2), 319-28.
- Park, J. et al. (1999) EMBO J 18, 3024-33.
- Brunet, A. et al. (2001) Mol Cell Biol 21, 952-65.
- Mikosz, C.A. et al. (2001) J Biol Chem 276, 16649-54.
- Hayashi, M. et al. (2001) J Biol Chem 276, 8631-4.
- Brickley, D.R. et al. (2002) J Biol Chem 277, 43064-70.
- Vasudevan, K.M. et al. (2009) Cancer Cell 16, 21-32.
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For Research Use Only. Not For Use In Diagnostic Procedures.