EPH Receptor A4, also known as EphA4, is a member of the ephrin receptor subfamily of the protein-tyrosine kinase family. This receptor is part of a larger family known as the Eph family, which includes 16 known receptors, 14 of which are found in mammals . EphA4 is a transmembrane receptor protein that plays a crucial role in various physiological and pathological processes, particularly in the nervous system and erythropoiesis .
EphA4 is a receptor tyrosine kinase that binds to membrane-bound ephrin family ligands on adjacent cells. This binding leads to contact-dependent bidirectional signaling into neighboring cells . The Eph family of receptors is divided into two classes: EphA and EphB, based on their ligand-binding preferences. EphA4, specifically, binds to ephrin-A ligands .
The extracellular domain of EphA4 interacts with ephrin ligands, which may be tethered to neighboring cells. This ligand-mediated activation induces various important downstream effects, including the regulation of synaptic function and plasticity . EphA4 is enriched on dendritic spines of pyramidal neurons in the adult mouse hippocampus, and ephrin-A3 is localized on astrocytic processes that envelop spines .
EphA4 has been extensively studied for its potential roles in the development of cancer and neurological diseases. It influences axonal and vascular guidance and has a widespread role in the pathological state of various central nervous system (CNS) disorders . Reports suggest that EphA4 obstructs axonal regeneration in various neurodegenerative diseases and neurological disorders . This makes EphA4 a potential therapeutic target for CNS diseases, as it may contribute to the course of neurodegenerative diseases through its associated signaling pathways .
Recombinant EphA4 proteins are typically expressed in HEK293 cells and are available in various forms, such as His-tagged proteins. These recombinant proteins are often lyophilized from sterile PBS and may contain protectants like trehalose, mannitol, and Tween80 . The purity of these proteins is generally high, with a purity of over 98% as determined by reducing SDS-PAGE .