Ephrin A3, also known as EFL-2, EHK1 ligand, EHK1-L, EPH-related receptor tyrosine kinase ligand 3, EFL2, EPLG3, and LERK3, is a member of the ephrin family of proteins. These proteins are cell surface glycosylphosphatidylinositol (GPI)-anchored ligands for Eph receptors, which are part of the largest subfamily of receptor protein-tyrosine kinases (RTKs). Ephrin A3 plays a crucial role in various biological processes, particularly in the nervous system and erythropoiesis .
Ephrin A3 is a GPI-bound ligand that binds promiscuously to Eph receptors on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells . The recombinant human Ephrin A3 protein is typically expressed in human 293 cells (HEK293) and carries a human IgG1 Fc tag at the C-terminus. The protein has a calculated molecular weight of approximately 48.4 kDa, but it migrates as 60-65 kDa under reducing conditions due to glycosylation .
Ephrin A3 is involved in several critical biological processes:
Due to its involvement in various biological processes, Ephrin A3 has potential clinical and translational applications. It is being studied for its role in cancer therapy, particularly in targeting tumor growth and metastasis. Additionally, its role in angiogenesis makes it a potential target for therapies aimed at promoting tissue repair and regeneration .
Recombinant human Ephrin A3 is produced using human 293 cells (HEK293) and is typically purified to a high degree of purity (>90%) as determined by SDS-PAGE. The protein is lyophilized from a filtered solution and can be reconstituted for use in various applications. It is essential to follow the specific reconstitution protocol provided to ensure optimal performance .
For long-term storage, the recombinant human Ephrin A3 protein should be stored in its lyophilized state at -20°C or lower. After reconstitution, it is stable for up to 3 months at -70°C under sterile conditions. It is crucial to avoid repeated freeze-thaw cycles to maintain the protein’s stability and activity .