Product Name: KinSub4RRLSL
Product Number: PE-01AKX95
Size: 200 µg      Price:99.00
      $US
Peptide Name: KinSub4RRLSL

Product Use: For assaying the phosphotransferase activity of Ephrin type-B receptor 1 protein-tyrosine kinase (EphB1, UniProt ID P54762). The KinSub4RRLSL peptide demonstrated high phosphotransferase activity with EphB1, 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: KinSub4RRLSL 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: GGRGRRLSLYQGRYG

Peptide Modifications N Terminus: Free amino

Peptide Modifications C Terminus: Amide

Peptide Molecular Mass Calculated: 1694.9 Da

Peptide Purity Percent after Synthesis and Purification: >95

Peptide Appearance: White powder

Peptide Form: Solid

Storage Conditions: -20°C

Peptide Recommended Enzyme: EphB1

Scientific Background: EphB1 is one of several protein kinases that can phosphorylate KinSub4RRLSL. Human EphB1 is a receptor protein-tyrosine kinase of 984 amino acid length, with a predicted molecular mass of 109,885 Da. It is a member of the TK group of protein kinases in the Eph family. This kinase is moderate to highly expressed in most tested human tissues. Orthologues of EphB1 are highly conserved in vertebrates and insects. EphB1 is activated by binding ephrin-B1, B2, or B3. The ligand-activated form interacts with Grb2, Grb10 and Nck through their respective SH2 domains. The GRB10 SH2 domain binds EphB1 through Y928, while GRB2 binds residues within the catalytic domain. The Nck SH2 domain binds EphB1 through Y594. Ligand-activated EphB1 induces tyrosine phosphorylation of paxillin in a Src-dependent manner to promote cell migration (1). In addition, activated EphB1 recruits the adaptor protein p52Shc and promotes p52Shc and c-Src tyrosine phosphorylation as well as MAPK/extracellular signal-regulated kinase (ERK) activation. Expression of dominant-negative c-Src significantly reduced EphB1-dependent ERK1/2 activation and chemotaxis (2). EphB1 has been linked with the development of gastric adenocarcinomas and ovarian undifferentiated carcinoma.