Product Name: KinSub2RRGSE
Product Number: PE-01AKB95
Size: | 200 µg | | Price: | 99.00 |
| | | $US | |
Peptide Name: KinSub2RRGSE
Product Use: For assaying the phosphotransferase activity of Protein-serine kinase C alpha (PKCa, UniProt ID P17252). The KinSub2RRGSE peptide demonstrated medium phosphotransferase activity with PKCi, and exhibited very high 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: KinSub2RRGSE 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: GGLSRRGSEGGGGGG
Peptide Modifications N Terminus: Free amino
Peptide Modifications C Terminus: Amide
Peptide Molecular Mass Calculated: 1259.3 Da
Peptide Purity Percent after Synthesis and Purification: >95
Peptide Appearance: White powder
Peptide Form: Solid
Storage Conditions: -20°C
Peptide Recommended Enzyme: PKCi
Scientific Background: PKCa is one of several protein kinases that can phosphorylate KinSub2RRGSE. Human PKCa is a protein-serine/threonine kinase of 672 amino acid length, with a predicted molecular mass of 76,764 Da. It is a member of the AGC group of protein kinases in the PKC family, and Alpha subfamily. This kinase is moderate to highly expressed in most tested human tissues. Orthologues of PKCa are highly conserved in vertebrates and insects. PKCa regulates many different cellular processes, including cell adhesion, cell transformation, cell cycle checkpoint, and cell volume control (1). PKCa is activated by binding of calcium, diacylglycerol and phosphatidylserine. Fatty acids can also activate PKCa. Phosphorylation of T494, T495 and T497 increases kinase activity. Phosphorylation of S657 increases phosphotransferase activity, protects against dephosphorylation of the T497 site and degradation of PKC-alpha. Phosphorylation of T638 is not essential for catalytic activity, but it protects against dephosphorylation of the T497 site. PKCa has been assigned to the chromosome region 17q22-q23.2 and has been identified as a fundamental regulator of cardiac contractility and Ca(2+) handling in myocytes (2). PKCa has been linked with the development of colon, pituitary and thyroid cancers as well as glioblastoma multiforme (GM).
References[1] Coussens L, Parker PJ, Rhee L, Yang-Feng TL, Chen E, Waterfield MD, Francke U, Ullrich A. Multiple, distinct forms of bovine and human protein kinase C suggest diversity in cellular signaling pathways. Science. 1986 Aug 22;233(4766):859-66. PMID: 3755548[2] Braz JC, Gregory K, Pathak A, Zhao W, Sahin B, Klevitsky R, Kimball TF, Lorenz JN, Nairn AC, Liggett SB, Bodi I, Wang S, Schwartz A, Lakatta EG, DePaoli-Roach AA, Robbins J, Hewett TE, Bibb JA, Westfall MV, Kranias EG, Molkentin JD. PKC-alpha regulates cardiac contractility and propensity toward heart failure. Nat Med. 2004 Mar;10(3):248-54. Epub 2004 Feb 15. PMID: 14966518