Product Name: KinSubaRRGSF
Product Number: PE-01ALR95
Size: 200 µg      Price:99.00
      $US
Peptide Name: KinSubaRRGSF

Product Use: For assaying the phosphotransferase activity of Serine/arginine-rich protein-specific kinase 2; Serine kinase SRPK2 (SRPK2, UniProt ID P78362). The KinSubaRRGSF peptide demonstrated high 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: KinSubaRRGSF 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: GGRGRRGSFCNGGHY

Peptide Modifications N Terminus: Free amino

Peptide Modifications C Terminus: Amide

Peptide Molecular Mass Calculated: 1579.7 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: SRPK2 is one of several protein kinases that can phosphorylate KinSubaRRGSF. Human SRPK2 is a protein-serine/threonine kinase of 688 amino acid length, with a predicted molecular mass of 77,543 Da. It is a member of the CMGC group of protein kinases in the SRPK family. This kinase is moderate to highly expressed in most tested human tissues. Orthologues of SRPK2 are amongst the most highly conserved protein kinases in animals, plants, fungi and unicellular eukaryotes. SRPK2 is a member of the serine/arginine (SR) protein-specific kinase family that are cell cycle-regulated protein kinases which phosphorylate SR domain-containing proteins in nuclear speckles and mediate the pre-mRNA splicing events (1). SRPK2 is activated by phosphorylation at S52 and S588. SRPK2 knock down results in hypophosphorylation of the serine/arginine domain-containing human PRP28 protein thereby destabilizing PRP28 association with the tri-snRNP. RNAi-mediated depletion in HeLa cells showed that SRPK2 is essential for cell viability, and it is required for spliceosomal B complex formation (2). SRPK2 has been linked with the development of glioblastoma multiforme (GM).