Product Pathways - PI3K / Akt Signaling
Phospho-SGK (Ser78) Antibody #3271
|W||H (M) (R)||Transfected Only||54 (Transfected only)||Rabbit|
Reactivity Key: H=Human M=Mouse R=Rat
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.
Specificity / Sensitivity
Phospho-SGK (Ser78) Antibody detects transfected levels of SGK1 only when phosphorylated at serine 78. It will not detect isoforms SGK2 or SGK3.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser78 of human SGK. Antibodies are purified by protein A and peptide affinity chromatography.
Western blot analysis of extracts from HeLa cells untransfected (left lane) and transfected by HA-SGK (right lane), using Phospho-SGK (Ser78) Antibody (upper) or control SGK Antibody #3272 (lower). The phospho-specificity of the antibody was characterized by treating the membrane with or without calf intestinal alkaline phosphatase (CIP) after Western transfer.
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).
The MAP kinase family member BMK1 interacts with and activates SGK by phosphorylation at serine 78 (6).
- 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.
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For Research Use Only. Not For Use In Diagnostic Procedures.