Product Name: KinSub6RRKSF
Product Number: PE-01ALG95
Size: | 200 µg | | Price: | 99.00 |
| | | $US | |
Peptide Name: KinSub6RRKSF
Product Use: For assaying the phosphotransferase activity of Lymphokine-activated killer T-cell-originated protein kinase (PBK, UniProt ID Q96KB5). The KinSub6RRKSF peptide demonstrated medium phosphotransferase activity with PBK, and exhibited 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: KinSub6RRKSF 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: GFRGRRKSFCVSGHG
Peptide Modifications N Terminus: Free amino
Peptide Modifications C Terminus: Amide
Peptide Molecular Mass Calculated: 1649.9 Da
Peptide Purity Percent after Synthesis and Purification: >95
Peptide Appearance: White powder
Peptide Form: Solid
Storage Conditions: -20°C
Peptide Recommended Enzyme: PBK
Scientific Background: PBK is one of several protein kinases that can phosphorylate KinSub6RRKSF. Human PBK (also known as TOPK) is a protein-serine/threonine kinase of 322 amino acid length, with a predicted molecular mass of 36,085 Da. It is a member of the Other group of protein kinases in the TOPK family. This kinase shows high variability in human tissue distribution with the highest levels detected in lymph nodes, pituitary, spleen, testes and tonsils. Expression of TOPK is particularly detected in male germ line progenitor cells, activated T-cells, and a variety of lymphomas and leukemias. Orthologues of PBK are highly conserved in vertebrates and insects. T9 phosphorylation of PBK by CDK1 increases its phosphotransferase activity and induces interaction with CCNB1, CDK1, and tubulin-alpha1. TOPK phosphorylates p38 MAPK (but not JNK or ERK1/2) and is activated in a cell-cycle-dependent manner in neuronal progenitor cells in vitro (1). TOPK activation requires phosphorylation by both the M-phase CDK1/CyclinB kinase complex and another unknown kinase, possibly RafC or RafA. TOPK may play an important role in linking extracellular signals to an intracellular state, possibly allowing extracellular influence on the cell-cycle-related processes of proliferation or differentiation (2).
References[1] Matsumoto S, Abe Y, Fujibuchi T, Takeuchi T, Kito K, Ueda N, Shigemoto K, Gyo K. Characterization of a MAPKK-like protein kinase TOPK. Biochem Biophys Res Commun. 2004 Dec 17;325(3):997-1004. PMID: 15541388[2] Simons-Evelyn M, Bailey-Dell K, Toretsky JA, Ross DD, Fenton R, Kalvakolanu D, Rapoport AP. PBK/TOPK is a novel mitotic kinase which is upregulated in Burkitt's lymphoma and other highly proliferative malignant cells. Blood Cells Mol Dis. 2001 Sep-Oct;27(5):825-9. PMID:11783945