Product Name: KinSub1RRGSL
Product Number: PE-01AJC95
Size: | 200 µg | | Price: | 99.00 |
| | | $US | |
Peptide Name: KinSub1RRGSL
Product Use: For assaying the phosphotransferase activity of Aurora Kinase A (AurA, Serine/threonine protein kinase 6, UniProt ID O14965). The KinSub1RRGSL peptide demonstrated very high phosphotransferase activity with PKCg, 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: KinSub1RRGSL 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: RGLGRRGSLGFFFGW
Peptide Modifications N Terminus: Free amino
Peptide Modifications C Terminus: Amide
Peptide Molecular Mass Calculated: 1712 Da
Peptide Purity Percent after Synthesis and Purification: >95
Peptide Appearance: White powder
Peptide Form: Solid
Storage Conditions: -20°C
Peptide Recommended Enzyme: PKCg
Scientific Background: AurA (AurKA, AIK) is a protein-serine/threonine kinase of the Other group and AUR family. It regulates cell cycle progression, and it mediates chromosomal segregation during mitosis. AurA phosphotransferase activity is greatest during mitosis. It is activated by phosphorylation at S284, T287, T288 and S342. AurA appears to be a tumour requiring protein (TRP). The active form of the protein kinase normally acts to promote tumour cell proliferation. Although AurA is not an oncoprotein, it is required for upstream oncoproteins to promote tumour formation. Its low rate of mutation and down-regulation in human cancers supports it identification as a TRP, and as a target for cancer drug development. However, the overexpression of AURA has been well documented in many malignant cancers including breast, ovarian, colon, prostate and neuroblastomas. Overexpression of AURA appears to override checkpoints in cell cycle progression leading to increased cell division and proliferation. Its phosphotransferase activity is decreased 10-fold with G198N (which also induces abnormal binding to INCENP and BIRC5), or increased with T288D. Phosphatase type I interactions could be decreased with F165A, and F346A mutations, while ubiquitination could be reduced with R205A. Autophosphorylation is inhibited with D274N, and TPX2 interactions are interrupted with a T287E mutation.