Cell Signaling Technology

Product Pathways - Glucose Metabolism

Phospho-SGK1 (Thr256) Antibody #2939

Applications Reactivity MW (kDa) Source
W H M 50 Rabbit

Applications Key:  W=Western Blotting
Reactivity Key:  H=Human  M=Mouse
Species enclosed in parentheses are predicted to react based on 100% sequence homology. Species cross-reactivity is determined by Western blot.

Specificity / Sensitivity

Phospho-SGK1 (Thr256) Antibody detects endogenous levels of SGK1 only when phosphorylated at Thr256. The antibody also detects recombinant human SGK2 when phosphorylated at Thr253.

Source / Purification

Polyclonal antibodies are produced by immunizing rabbits with a synthetic phosphopeptide (KLH-coupled) derived from residues surrounding Thr256 of mouse SGK1.

Western Blotting

Western Blotting

Western blot analysis of extracts from HeLa at either G1/S cell cycle stage (hydroxyurea 4 mM, 20 hours) or at G2/M cell cycle stage (paclitaxel 100 nM/ml, 20 hrs), using Phospho-SGK1 (Thr256) Antibody (upper) or β-Actin Antibody #4967 (lower) to show induction of phospho-SGK and equal loading.

Background

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 antiapoptotic 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 ubiquitin modification and proteasome degradation (7).

SGK is phosphorylated in vitro and in vivo by PDK1 on Thr256 in its activation loop. This phosphorylation leads to the activation of SGK1 mediated by PI3 kinase signaling (3).

  1. Webster, M.K. et al. (1993) Mol. Cell. Biol. 13, 2031-2040.
  2. Kobayashi, T. and Cohen, P. (1999) Biochem. J. 339, 319-328.
  3. Park, J. et al. (1999) EMBO J. 18, 3024-3033.
  4. Brunet, A. et al. (2001) Mol. Cell. Biol. 21, 952-965.
  5. Mikosz, C.A. et al. (2001) J. Biol. Chem. 276, 16649-16654.
  6. Hayashi, M. et al. (2001) J. Biol. Chem. 276, 8631-8634.
  7. Brickley, D.R. et al. (2002) J. Biol. Chem. 277, 43064-43070.

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