Product Name: KinSub1DDDYP
Product Number: PE-01AGL95
| Size: | 200 µg | Price: | 99.00 | |
| $US |
Peptide Name: KinSub1DDDYP
Product Use: For assaying the phosphotransferase activity of Ephrin type-B receptor 2 protein-tyrosine kinase (EphB2, UniProt ID P29323). The KinSub1DDDYP peptide demonstrated high phosphotransferase activity with Brk, and exhibited high 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: KinSub1DDDYP 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: EGLEDDDYPYPGGGG
Product Use: For assaying the phosphotransferase activity of Ephrin type-B receptor 2 protein-tyrosine kinase (EphB2, UniProt ID P29323). The KinSub1DDDYP peptide demonstrated high phosphotransferase activity with Brk, and exhibited high 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: KinSub1DDDYP 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: EGLEDDDYPYPGGGG
Peptide Modifications N Terminus: Free amino
Peptide Modifications C Terminus: Amide
Peptide Molecular Mass Calculated: 1539.5 Da
Peptide Purity Percent after Synthesis and Purification: >95
Peptide Appearance: White powder
Peptide Form: Solid
Storage Conditions: -20°C
Peptide Recommended Enzyme: Brk
Peptide Modifications C Terminus: Amide
Peptide Molecular Mass Calculated: 1539.5 Da
Peptide Purity Percent after Synthesis and Purification: >95
Peptide Appearance: White powder
Peptide Form: Solid
Storage Conditions: -20°C
Peptide Recommended Enzyme: Brk
Scientific Background: EphB2 is one of several protein kinases that can phosphorylate KinSub1DDDYP. Human EphB2 is a receptor protein-tyrosine kinase of 1055 amino acid length, with a predicted molecular mass of 117,493 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 EphB2 are highly conserved in vertebrates, including amphibians. EphB2 is activated by binding ephrin-B1, B2, or B3. The ligand-activated form interacts with multiple proteins, including GTPase-activating protein (RASGAP) through its SH2 domain and RASGAP through the juxtamembrane tyrosines residues. EphB2 mediates neurodevelopmental processes such as boundary formation, axon guidance, vasculogenesis, and cell migration. EphB2 has been shown to associate with the non-receptor tyrosine kinase Abl and activated EphB2 causes tyrosine phosphorylation of Abl and regulates its activity (1). EphB2 is overexpressed in a number of tumors particularly glioblastoma and this increases glioma cell migration and invasion (2). EphB2 has also been linked with the development of breast and prostate cancers.
References
[1] Yu HH, Zisch AH, Dodelet VC, Pasquale EB. Multiple signaling interactions of Abl and Arg kinases with the EphB2 receptor. Oncogene. 2001 Jul 5;20(30):3995-4006. PMID: 11494128
[2] Nakada M, Niska JA, Miyamori H, McDonough WS, Wu J, Sato H, Berens ME. The phosphorylation of EphB2 receptor regulates migration and invasion of human glioma cells. Cancer Res. 2004 May 1;64(9):3179-85. PMID:15126357
[1] Yu HH, Zisch AH, Dodelet VC, Pasquale EB. Multiple signaling interactions of Abl and Arg kinases with the EphB2 receptor. Oncogene. 2001 Jul 5;20(30):3995-4006. PMID: 11494128
[2] Nakada M, Niska JA, Miyamori H, McDonough WS, Wu J, Sato H, Berens ME. The phosphorylation of EphB2 receptor regulates migration and invasion of human glioma cells. Cancer Res. 2004 May 1;64(9):3179-85. PMID:15126357
© Kinexus Bioinformatics Corporation 2017