EPHB2 is a transmembrane protein consisting of 1,055 amino acids and has a molecular weight of approximately 117 kDa . It is encoded by the EPHB2 gene located on chromosome 1p36.12 in humans . The receptor is characterized by an extracellular region containing a ligand-binding domain, a cysteine-rich domain, and two fibronectin type III repeats. The intracellular region includes a tyrosine kinase domain, a sterile alpha motif (SAM), and a PDZ-binding motif .
EPHB2 binds promiscuously to ephrin-B family ligands, which are also transmembrane proteins. This binding leads to contact-dependent bidirectional signaling, where the signaling pathway downstream of the receptor is referred to as forward signaling, and the pathway downstream of the ephrin ligand is referred to as reverse signaling .
EPHB2 is involved in several critical developmental processes:
Recombinant human EPHB2 protein is often used in research to study its function and interactions. It is typically expressed in baculovirus-infected Sf9 cells and purified to a high degree of purity (>95%) for use in various applications such as SDS-PAGE and functional assays . The recombinant protein retains its biological activity, making it a valuable tool for studying EPHB2-mediated signaling pathways.