Product Name: KinSub1DGNYV
Product Number: PE-01AGY95
Size: 200 µg      Price:99.00
      $US
Peptide Name: KinSub1DGNYV

Product Use: For assaying the phosphotransferase activity of Ephrin type-A receptor 4 (EphA4, UniProt ID P54764). The KinSub1DGNYV peptide demonstrated high phosphotransferase activity with Blk, 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: KinSub1DGNYV 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: GLGEDGNYVGVCPGY

Peptide Modifications N Terminus: Free amino
Peptide Modifications C Terminus: Amide

Peptide Molecular Mass Calculated: 1498.6 Da

Peptide Purity Percent after Synthesis and Purification: >95

Peptide Appearance: White powder

Peptide Form: Solid

Storage Conditions: -20°C

Peptide Recommended Enzyme: Blk

Scientific Background: EphA4 is one of several protein kinases that can phosphorylate KinSub1DGNYV. Human EphA4 is a receptor protein-tyrosine kinase of 986 amino acid length, with a predicted molecular mass of 109,860 Da. It is a member of the TK group of protein kinases in the Eph family. This kinase is highly expressed and widely distributed in most tested human tissues. Orthologues of EphA4 are highly conserved in vertebrates, including amphibians. Phosphorylation of EphA4 at Y602 interaction with Fyn. Phosphorylation at Y928 inhibits EphA4 phosphotransferase activity. EphA4 has been implicated in mediating developmental events, particularly in the nervous system (1). The EphA4 ligand ephrin-A3 is localized to the astrocytic processes that envelop the spine. Activation of EphA4 by ephrin-A3 induces spinal retraction and reduces spine density and inhibits the interaction distorted spine shape and organization. EphA4-null mice possess defects in the corticospinal tract and anterior commissure indicating a model in which an ephrin ligand on the axons senses EphA4 on spinal cord cells surrounding the corticospinal tract (2). EphA4 has been linked with the development of bladder carcinomas and melanoma (metastatic).