SKG-1 Antibody

Background

SGK-1 (also called Serine/threonine-protein kinase Sgk1 and Serum/glucocorticoid-regulated kinase 1) is a protein kinase that plays an important role in cellular stress response.  SGK1 activates certain potassium, sodium, and chloride channels, suggesting an involvement in the regulation of processes such as cell survival, neuronal excitability, and renal sodium excretion. Sustained high levels and activity may contribute to conditions such as hypertension and diabetic nephropathy. This kinase mediates cell survival signals, phosphorylates and negatively regulates pro-apoptotic FOXO3A and phosphorylates NEDD4L, which leads to its inactivation and to the subsequent activation of various channels and transporters such as ENaC, Kv1.3, or EAAT1. SGK1 is localized to the cytoplasm and upon phosphorylation is translocated to the nucleus.  The kinase is expressed in most tissues with highest levels in the pancreas, followed by placenta, kidney and lung.  Induction occurs upon exposure to glucocorticoids and by excessive extracellular glucose or TGF-beta, in cultured cells.   SGK-1 is regulated by phosphorylation.  Phosphoinositide 3-kinase (PI3-kinase) pathway promotes phosphorylation at Ser-422 which in turn increases the phosphorylation of Thr-256 by PDPK1. The kinase is ubiquitinated by NEDD4L; which promotes proteasomal degradation.