Product Name: KinSubcRRGSF
Product Number: PE-01ALU95
| Size: | 200 µg | Price: | 99.00 | |
| $US |
Peptide Name: KinSubcRRGSF
Product Use: For assaying the phosphotransferase activity of Checkpoint protein-serine kinase 2 (CHK2, UniProt ID O96017). The KinSubcRRGSF peptide demonstrated very low phosphotransferase activity with Pim1, 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: KinSubcRRGSF 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: GGRSRRGSFCHKTGG
Product Use: For assaying the phosphotransferase activity of Checkpoint protein-serine kinase 2 (CHK2, UniProt ID O96017). The KinSubcRRGSF peptide demonstrated very low phosphotransferase activity with Pim1, 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: KinSubcRRGSF 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: GGRSRRGSFCHKTGG
Peptide Modifications N Terminus: Free amino
Peptide Modifications C Terminus: Amide
Peptide Molecular Mass Calculated: 1561.8 Da
Peptide Purity Percent after Synthesis and Purification: >95
Peptide Appearance: White powder
Peptide Form: Solid
Storage Conditions: -20°C
Peptide Recommended Enzyme: Pim1
Peptide Modifications C Terminus: Amide
Peptide Molecular Mass Calculated: 1561.8 Da
Peptide Purity Percent after Synthesis and Purification: >95
Peptide Appearance: White powder
Peptide Form: Solid
Storage Conditions: -20°C
Peptide Recommended Enzyme: Pim1
Scientific Background: Chk2 is one of several protein kinases that can phosphorylate KinSubcRRGSF. Human Chk2 is a protein-serine/threonine kinase of 543 amino acid length, with a predicted molecular mass of 60,915 Da. It is a member of the CAMK group of protein kinases in the RAD53 family. This kinase shows high variability in human tissue distribution with the highest levels detected in spleen and tonsils, and is notably absent in brain and spinal cord. Orthologues of Chk2 are amongst the most highly conserved protein kinases in animals, plants, fungi and unicellular eukaryotes. Chk2 is activated by phosphorylation at T68 by MLTK in response to replication blocks and DNA damage; the response to DNA damage occurs in an ataxia telangiectasia mutated (ATM)-dependent manner (1). It is also activated by phosphorylation at S19, T26, S28, S33, S35, T383, T387 and S516. Expression of wild-type Chk2 leads to increased p53 stabilization after DNA damage, whereas expression of a dominant-negative Chk2 mutant abrogated both phosphorylation of p53 on S20 and p53 stabilization (2). Chk2 has been linked with the development of Li-Fraumeni Syndrome 2 (LFS2), breast, colon, and prostate cancers, and osteosarcomas.
References
[1] Matsuoka S, Huang M, Elledge SJ. Linkage of ATM to cell cycle regulation by the Chk2 protein kinase. Science. 1998 Dec 4;282(5395):1893-7. PMID: 9836640.
[2] Chehab NH, Malikzay A, Appel M, Halazonetis TD. Chk2/hCds1 functions as a DNA damage checkpoint in G(1) by stabilizing p53. Genes Dev. 2000 Feb 1;14(3):278-88. PMID: 10673500.
[1] Matsuoka S, Huang M, Elledge SJ. Linkage of ATM to cell cycle regulation by the Chk2 protein kinase. Science. 1998 Dec 4;282(5395):1893-7. PMID: 9836640.
[2] Chehab NH, Malikzay A, Appel M, Halazonetis TD. Chk2/hCds1 functions as a DNA damage checkpoint in G(1) by stabilizing p53. Genes Dev. 2000 Feb 1;14(3):278-88. PMID: 10673500.
© Kinexus Bioinformatics Corporation 2017