Product Name: KinSub5RRLSP
Product Number: PE-01ALD95
Size: 200 µg      Price:99.00
      $US
Peptide Name: KinSub5RRLSP

Product Use: For assaying the phosphotransferase activity of Serine/arginine-rich protein-specific kinase 1 (SRPK1, UniProt ID Q96SB4). The KinSub5RRLSP peptide demonstrated high phosphotransferase activity with CHK2, 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: KinSub5RRLSP 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: GGRSRRLSPGGGGYW

Peptide Modifications N Terminus: Free amino

Peptide Modifications C Terminus: Amide

Peptide Molecular Mass Calculated: 1561.7 Da

Peptide Purity Percent after Synthesis and Purification: >95

Peptide Appearance: White powder

Peptide Form: Solid

Storage Conditions: -20°C

Peptide Recommended Enzyme: CHK2

Scientific Background: SRPK1 is one of several protein kinases that can phosphorylate KinSub5RRLSP. Human SRPK1 is a protein-serine/threonine kinase of 655 amino acid length, with a predicted molecular mass of 74,325 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 except apparently in the brain and spinal cord. Orthologues of SRPK1 are highly conserved in animals and plants. SRPK1 is activated by phosphorylation at S51 and S555. In human cancer cells, it was observed that inactivation of SRPK1 induces cellular resistance to anticancer drugs such as cisplatin and bleomycin (1). SRPK1 phosphorylates serine/arginine-rich (SR) proteins, such as splicing factors ASF/SF2, SC35, and SRp55, in their arginine/serine-rich (RS) domains in vitro. Consequently, it is believed that SRPK1 plays a key role in regulation of both constitutive and alternative splicing by regulating intracellular localization of splicing factors (2).