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Background: The SGK family belongs to the AGC class of kinases and consists of three members; SGK1, SGK2 and SGK3. While SGK1 and SGK3 are ubiquitously expressed in all tissues, SGK2 is primarily expressed only in liver, kidney, and pancreas. SGK expression is rapidly induced by serum and glucocorticoid. Similar to its isoforms SGK2 and SGK3, SGK1 is activated by insulin and growth factors via phosphatidylinositol 3-kinase and the 3-phosphoinositide-dependent kinase PDK1. SGK1 activates ion channels and contributes to Na+ retention and K+ elimination of the kidney, glucocorticoid stimulation of intestinal Na+/H+ exchanger and nutrient transport. Additionally, SGK1 regulates the activity of several enzymes (e.g., glycogen-synthase-kinase-3, ubiquitin-ligase Nedd4-2, phosphomannose-mutase-2), and transcription factors (e.g., forkhead-transcription-factor FOXO3a, β-catenin and NF-κB). Since a SGK1 gene variant is associated with increased blood pressure and body weight the enzyme may contribute to metabolic syndrome. Furthermore, SGK1 is a potent negative regulator of TLR-induced inflammation and inhibition or suppression of SGK1 enhances proinflammatory cytokine (TNF, IL-12, and IL-6) production in TLR-engaged monocytes.
Recombinant human protein kinase SGK1 (serum/glucocorticoid regulated kinase), amino acids M1-L431, recombinant and active enzyme, N-terminally fused to GST, activated by PDK1
Theoretical MW : 74.950 kDa (fusion proteins)
Expression system: Baculovirus infected Sf9 cells
Purification: One-step affinity purification using GSH-agarose
Storage buffer: 50 Hepes, pH 7.5; 100 mM NaCl, 5 mM DTT, 15 mM reduced glutathione, 20% glycerol
Protein concentration: 0.126 mg/ml (Bradford method using BSA as standard protein)
Method for determination of Km value & specific activity: Filter binding assay MSPH membrane
Specific activity: 54,000 pmol/mg min
Entrez Gene ID: 6446
UniProtKB: O00141
Ordering informations: shipped on dry ice
H. Zhou, S. Gao, X. Duan, S. Liang, D.A. Scott, R.J. Lamont, H. Wang (2015) “Inhibition of serum- and glucocorticoid-inducible kinase 1 enhances TLR-mediated inflammation and promotes endotoxin-driven organ failure” FASEB J., 29, pp. 3737–3749
F. Lang, C. Bohmer, M. Palmada, G. Seebohm, N. Strutz-Seebohm, V. Vallon (2006) „Patho)physiological significance of the serum- and glucocorticoid-inducible kinase isoforms” Physiol. Rev., 86 pp. 1151–1178
F. Lang, A. Gorlach, V. Vallon (2009) „Targeting SGK1 in diabetes” Expert Opin. Ther. Targets, 13, pp. 1303–1311
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