EphB2, also known as Cek5, Nuk, Erk, Qek2, Tyro5, Sek3, Hek5, and Drt (1), is a member of the Eph receptor family which binds members of the ephrin ligand family. There are two classes of receptors, designated A and B. Both the A and B class receptors have an extracellular region consisting of a globular domain, a cysteine-rich domain, and two fibronectin type III domains. This is followed by the transmembrane region and the cytoplasmic region. The cytoplasmic region contains a juxtamembrane motif with two tyrosine residues which are the major autophosphorylation sites, a kinase domain, and a conserved sterile alpha motif (SAM) in the carboxy tail which contains one conserved tyrosine residue. Activation of kinase activity occurs after ligand recognition and binding. EphB2 has been shown to bind ephrin-B1, ephrin-B2, and ephrin-B3 (2, 3). The extracellular domains of human and mouse EphB2 share 99% amino acid identity. Only membrane-bound or Fc‑clustered ligands are capable of activating the receptor in vitro. Soluble monomeric ligands bind the receptor but do not induce receptor autophosphorylation and activation (2). In vivo, the ligands and receptors display reciprocal expression (3). It has been found that nearly all the receptors and ligands are expressed in developing and adult neural tissue (3). The ephrin/Eph families also appear to play a role in angiogenesis (3).