Cell Signaling Technology

Product Pathways - PI3K / Akt Signaling

SGK3 (D42C2) Rabbit mAb #8573

Applications Reactivity Sensitivity MW (kDa) Isotype
W IP H M R Mk Endogenous 61 Rabbit IgG

Applications Key:  W=Western Blotting  IP=Immunoprecipitation
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.

Protocols

Specificity / Sensitivity

SGK3 (D42C2) Rabbit mAb recognizes endogeneous levels of total SGK3 protein.

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Tyr487 of human SGK3 protein.

Western Blotting

Western Blotting

Western blot analysis of extracts from various cell lines using SGK3 (D42C2) Rabbit mAb.

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 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 has been suggested to be an Akt-independent manner of signaling in cancer (8).

  1. Webster, M.K. et al. (1993) Mol Cell Biol 13, 2031-40.
  2. Kobayashi, T. and Cohen, P. (1999) Biochem J 339 ( Pt 2), 319-28.
  3. Park, J. et al. (1999) EMBO J 18, 3024-33.
  4. Brunet, A. et al. (2001) Mol Cell Biol 21, 952-65.
  5. Mikosz, C.A. et al. (2001) J Biol Chem 276, 16649-54.
  6. Hayashi, M. et al. (2001) J Biol Chem 276, 8631-4.
  7. Brickley, D.R. et al. (2002) J Biol Chem 277, 43064-70.
  8. Vasudevan, K.M. et al. (2009) Cancer Cell 16, 21-32.

Application References

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For Research Use Only. Not For Use In Diagnostic Procedures.

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