Product Name: KinSub1FPLSP
Product Number: PE-01AHD95
Size: | 200 µg | | Price: | 99.00 |
| | | $US | |
Peptide Name: KinSub1FPLSP
Product Use: For assaying the phosphotransferase activity of Cyclin-dependent protein-serine kinase 2 (CDK2, UniProt ID P24941). The KinSub1FPLSP peptide demonstrated high phosphotransferase activity with CDK2, 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: KinSub1FPLSP 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: GGGSFPLSPGKKGGG
Peptide Modifications N Terminus: Free amino
Peptide Modifications C Terminus: Amide
Peptide Molecular Mass Calculated: 1301.5 Da
Peptide Purity Percent after Synthesis and Purification: >95
Peptide Appearance: White powder
Peptide Form: Solid
Storage Conditions: -20°C
Peptide Recommended Enzyme: CDK2
Scientific Background: CDK2 is a protein-serine/threonine kinase of the CMGC group and CDK family. It is essential for meiosis, yet not essential for mitosis, although it is involved in cell cycle control. CDK2 has been observed to phosphorylate CTNNB1, USP37, p53/TP53, NPM1, CDK7, RB1, BRCA2, MYC, NPAT, and EZH2. Involved in the control of the cell cycle. Interacts with cyclins A, B1, B3, D, or E. Activity of CDK2 is maximal during S phase and G2. Mutations resulting in reduced CAK phosphorylation at the T160 activating phosphosite include K9F, and K88E + K89V, while a L166R mutation results in reduced CAK phosphorylation and lower protein-serine/threonine phosphotransferase activity. Phosphorylation at Y179 increases phosphotransferase activity and interaction with CCNA2 (Cyclin A2). CCNA2 stimulates the catalytic activity of CDK2. Phosphorylation at T14 and Y15 inhibits phosphotransferase activity.
References[1] Levkau B, Koyama H, Raines EW, Clurman BE, Herren B, Cleavage of p21Cip1/Waf1 and p27Kip1 mediates apoptosis in endothelial cells through activation of Cdk2: role of a caspase cascade. Orth K, Roberts JM, Ross R. Mol Cell. 1998 Mar;1(4):553-63. PMID: 9660939.[2] Huang H, Regan KM, Lou Z, Chen J, Tindall DJ. CDK2-dependent phosphorylation of FOXO1 as an apoptotic response to DNA damage. Science. 2006 Oct 13;314(5797):294-7. PMID: 17038621.