EphA7 antibody

EphA7, also known as Mdk1, Hek11, Ehk3, Ebk, and Cek11, 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 is a juxtamembrane region with two tyrosines, the major autophosphorylation sites, along with a kinase domain, and a conserved sterile alpha motif (SAM) in the C-terminus, the latter including one conserved tyrosine. The extracellular domains of human and mouse EphA7 share 97% amino acid identity. The calculated molecular mass of the reduced mouse EphA7/Fc monomer is 85.7 kDa, but as a result of glycosylation, recombinant EphA7/Fc migrates as an approximately 110 kDa protein under reducing conditions in SDS-PAGE.Ligand recognition and binding leads to activation of the intrinsic kinase activity. EphA7 binds to ephrin A1, ephrin A2, ephrin A3, ephrin A4, and ephrin A5. 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.