EphB2 antibody

EphB2, also known as Cek5, Hek5, Tyro5, Se3, Nuk, Erk, Qek2, and Drt, is a member of the Eph receptor family, which binds members of the ephrin ligand family. Two classes of receptors exist, designated A and B, that have an extracellular domain made up of a globular domain, a cysteine-rich domain, and two fibronectin type III domains, followed by the transmembrane region and cytoplasmic region. The cytoplasmic region contains a juxtamembrane motif with two tyrosines, which are the major autophosphorylation sites, along with a kinase domain, and a conserved sterile alpha motif (SAM) in the carboxyl terminus, which includes one conserved tyrosine. The recombinant mouse EphB2 used for the testing of this antibody consists of the extracellular domain of mouse EphB2 (amino acids 1-548)1 fused by means of a polypeptide linker to the Fc portion of human IgG1 that is histidine-tagged at the C-terminus. N-terminal sequencing indicates that recombinant mouse EphB2 has Val 27 at the amino terminus. The calculated molecular mass of the reduced protein is approximately 85.3 kDa, but as a result of glycosylation, recombinantEphB2/Fc migrates as a 100-110 kDa protein under reducing conditions in SDS-PAGE. EphB2 binds to ephrin-B1, ephrin-B2, and ephrin-B3. Human and mouse EphB3 extracellular domains share approximately 99% homology. Ligand recognition and binding leads to activation of intrinsic kinase activity. Only membrane-bound or Fc-clustered ligands have been shown to activate the receptor in vitro. Soluble monomeric ligands can bind the receptor, but do not induce receptor autophosphorylation and activation. The ephrin ligands and Eph receptors display reciprocal expression in vivo. Developing and adult neural tissue express nearly all of the Eph receptors and ephrin ligands. Ephs and ephrins play a significant role in angiogenesis.