Recombinant Human EPHA3 protein

Eph receptor A3 (EPHA3) is a member of the Eph family of receptor tyrosine kinases, which play critical roles in cell-cell communication, tissue patterning, and developmental processes. Structurally, EPHA3 consists of an extracellular region with a ligand-binding domain, a cysteine-rich motif, and two fibronectin type III repeats, followed by a transmembrane helix and a cytoplasmic tyrosine kinase domain. It primarily interacts with membrane-bound ephrin-A ligands, initiating bidirectional signaling pathways that regulate cell adhesion, migration, and spatial organization. Dysregulation of EPHA3 has been implicated in various cancers, neurodegenerative diseases, and cardiovascular disorders, making it a potential therapeutic target.

Recombinant EPHA3 proteins are engineered in vitro to study its biological functions and interactions. These proteins are typically produced using mammalian expression systems (e.g., HEK293 or CHO cells) to ensure proper post-translational modifications, such as glycosylation. The recombinant form often includes the extracellular domain fused to tags like Fc or His for purification and detection. Researchers utilize EPHA3 recombinant proteins to investigate ligand-receptor binding kinetics, signal transduction mechanisms, and downstream effects in cellular assays. They also serve as critical tools for screening small-molecule inhibitors or antibodies aimed at modulating EPHA3 activity in disease contexts.

Quality control of recombinant EPHA3 involves verifying purity (>95% by SDS-PAGE), endotoxin levels, and functional validation through ligand-binding assays (e.g., ELISA or surface plasmon resonance). Its bioactivity is confirmed via phosphorylation assays or cell-based migration/invasion models. By enabling precise mechanistic studies, recombinant EPHA3 advances our understanding of its role in health and disease, supporting drug discovery and biomarker development efforts.