Product Name: KinSub1RRGSV
Product Number: PE-01AJE95
Size: | 200 µg | | Price: | 99.00 |
| | | $US | |
Peptide Name: KinSub1RRGSV
Product Use: For assaying the phosphotransferase activity of Serine/threonine-protein kinase Sgk2 (UniProt ID Q9HBY8). The KinSub1RRGSV peptide demonstrated medium phosphotransferase activity with Brk, and exhibited medium specificity when assayed with over 200 other protein kinases. A listing of other kinases that show appreciable phosphotransferase activity towards this peptide are listed in Table 1.
Peptide Production Method: Solid-phase peptide synthesis
Peptide Origin: KinSub1RRGSV was originally identified using a microarray with peptides that were predicted as optimal substrates for 500 human protein kinases with a proprietary algorithm developed at Kinexus with our academic partners.
Peptide Sequence: GGRGRRGSVCGGGYG
Peptide Modifications N Terminus: Free amino
Peptide Modifications C Terminus: Amide
Peptide Molecular Mass Calculated: 1394.5 Da
Peptide Purity Percent after Synthesis and Purification: >95
Peptide Appearance: White powder
Peptide Form: Solid
Storage Conditions: -20°C
Peptide Recommended Enzyme: Brk
Scientific Background: SGK2 is one of several protein kinases that can phosphorylate KinSub1RRGSV. Human SGK2 is a protein-serine/threonine kinase of 427 amino acid length, with a predicted molecular mass of 47,604 Da. It is a member of the AGC group of protein kinases in the SGK family (1). This kinase is moderate to highly expressed in most tested human tissues. Orthologues of SGK2 are amongst the most highly conserved protein kinases in animals, plants, fungi and unicellular eukaryotes. SGK2 is activated by phosphorylation at T253 and S416. SGK2 is serum- and glucocorticoid-induced. SGK2, like the other two isoforms SGK1 and SGK3, is stimulated by insulin and insulin-like growth factor-1 (IGF-1), and has been shown to enhance Na(+)/K(+)-ATPase activity in a variety of cells (2). SGK2 has been linked with the development of lung adenocarcinomas.
References[1] Kobayashi T, Deak M, Morrice N, Cohen P. Characterization of the structure and regulation of two novel isoforms of serum- and glucocorticoid-induced protein kinase. Biochem J. 1999 Nov 15;344 Pt 1:189-97. PMID: 10548550 PMCID: PMC1220630[2] Boehmer C, Embark HM, Bauer A, Palmada M, Yun CH, Weinman EJ, Endou H, Cohen P, Lahme S, Bichler KH, Lang F. Stimulation of renal Na+ dicarboxylate cotransporter 1 by Na+/H+ exchanger regulating factor 2, serum and glucocorticoid inducible kinase isoforms, and protein kinase B. Biochem Biophys Res Commun. 2004 Jan 23;313(4):998-1003. PMID: 14706641