Product Name: KinSub7RRKSF
Product Number: PE-01ALK95
Size: 200 µg      Price:99.00
      $US
Peptide Name: KinSub7RRKSF

Product Use: For assaying the phosphotransferase activity of Protein-serine kinase C beta 1 (PKCb2, UniProt ID P05771). The KinSub7RRKSF peptide demonstrated very high phosphotransferase activity with CHK2, and exhibited very low 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: KinSub7RRKSF 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: GGRFRRKSFRRKGHG

Peptide Modifications N Terminus: Free amino

Peptide Modifications C Terminus: Amide

Peptide Molecular Mass Calculated: 1801.1 Da

Peptide Purity Percent after Synthesis and Purification: >95

Peptide Appearance: White powder

Peptide Form: Solid

Storage Conditions: -20°C

Peptide Recommended Enzyme: CHK2

Scientific Background: PKCb2 is one of several protein kinases that can phosphorylate KinSub7RRKSF. Human PKCb is a protein-serine/threonine kinase of 671 amino acid length, with a predicted molecular mass of 76,869 Da. It is a member of the AGC group of protein kinases in the PKC family, and Alpha subfamily. It is moderate to highly expressed in most tested human tissues. Orthologues of PKCb are highly conserved in vertebrates and insects. PKCb is activated by calcium, diacylglycerol, and phosphatidylserine. Phosphorylation of T635 and T642 is critical for kinase activity. Phosphorylation of S661 inhibits membrane binding and causes release into cytoplasm. PKCbI is highly related to PKCbII. Unlike the mature PKCb II mRNA and protein, which rapidly increase following acute insulin treatment, the PKCbI mRNA and protein levels remain unchanged (1). Stable overexpression of PKCbII, but not PKCbI, leads to insulin-stimulated glucose uptake into cells. Upon stimulation of B cells and mast cells, Syk regulates Btk, and Btk selectively regulates enzymatic activity of PKCbI. Specific regulation of PKCbI by Btk is consistent with the selective association of Btk with PKCbI (2). PKCb has been linked with the development of diabetic nephropathy, colorectal adenocarcinomas and glioblastoma multiforme.