Recombinant human EPHB3, protein kinase domain,10 µg

Background: The Eph receptors are part of the receptor tyrosine kinases and can be divided into two classes, EphA and EphB, which respectively bind the glycosylphosphatidylinositol-linked ephrin-A ligands and the transmembrane ephrin-B ligands. Eph receptors and ephrin ligands interact through cell–cell contact, because they are bound to the plasma membrane. Thus, they activate bidirectional intracellular signaling emanating from both the receptor (forward signaling) and the ligand (reverse signaling). Upon ephrin binding, the Eph receptors are phosphorylated at specific tyrosine residues in the cytoplasmic region, serving as docking sites for various signaling molecules like Src, Grb2 and PI3K. Eph receptor signaling pathways target e.g. Rho GTPases, leading to the reorganization of the actin cytoskeleton and furthermore Eph receptors and ephrins can promote angiogenesis through their effects on endothelial cell migration as well as proliferation.

Recombinant human EPHB3 (Ephrin type-B receptor 3), amino acids Q585-V998, tyrosine kinase domain, recombinant and active enzyme, N-terminally fused to GST-HIS6-Thrombin cleavage site

Theoretical MW: 80.148 kDa (fusion protein)
Expression system: Baculovirus infected Sf9 cells
Purification: One-step affinity purification using GSH-agarose
Storage buffer: 50 mM Tris-HCl, pH 8.0;100 mM NaCl, 5 mM DTT, 15 mM reduced glutathione, 20% glycerol
Protein concentration: 0.258 mg/ml (Bradford method using BSA as standard protein)
Method for determination of Km value & specific activity: Filter binding assay MSFC membrane
Specific activity: 75,000 pmol/mg x min

Entrez Gene ID: 2049  
UniProtKB: P54753

Ordering information: shipped on dry ice

Product specific literature:

Schmucker D, Zipursky SL (2001) "Signaling downstream of Eph receptors and ephrin ligands.” Cell 15;105(6):701-4.

Noren NK, Pasquale EB (2007) “Paradoxes of the EphB4 receptor in cancer.” Cancer Res. 1;67(9):3994-7.

Nakamoto M, Bergemann AD (2002) "Diverse roles for the Eph family of receptor tyrosine kinases in carcinogenesis.” Microsc Res Tech. 1;59(1):58-67.