Recombinant Human SGK1 protein

Serum and glucocorticoid-regulated kinase 1 (SGK1) is a ubiquitously expressed serine/threonine protein kinase belonging to the AGC kinase family, sharing structural homology with AKT. First identified in 1993 as a glucocorticoid-responsive gene, SGK1 has emerged as a critical cellular regulator integrating hormonal and environmental signals. It is transcriptionally induced by serum, glucocorticoids, mineralocorticoids, and various stress stimuli, while its activity is post-translationally controlled via PI3K-dependent phosphorylation. Functionally, SGK1 modulates ion transport, cell survival, proliferation, and apoptosis by phosphorylating targets including Nedd4-2. ENaC, FOXO transcription factors, and MDM2. Its involvement in sodium homeostasis, neuroexcitability, and insulin signaling links it to hypertension, diabetes, cancer progression, and neurodegenerative disorders.

Recombinant SGK1 protein, typically produced in Escherichia coli or mammalian expression systems using genetic engineering techniques, serves as a vital tool for studying its enzymatic properties, substrate interactions, and inhibitor screening. The purified protein retains kinase activity and structural features of native SGK1. enabling in vitro phosphorylation assays and structural studies. Researchers utilize it to investigate SGK1's role in pathological mechanisms, particularly its overexpression in cancers promoting chemoresistance and metastasis, or its dysregulation in renal and cardiovascular diseases. Crystal structure analyses of recombinant SGK1 have revealed conformational changes during activation, while mutagenesis studies using recombinant variants help dissect phosphorylation-dependent regulatory mechanisms. Current therapeutic strategies targeting SGK1 in metabolic syndromes and drug-resistant tumors continue to drive demand for high-purity recombinant SGK1 in preclinical research.