Ephrin-A1/EFNA1 Protein, Rat (HEK293, His)

Ephrin-A1/EFNA1 protein, a cell surface GPI-bound ligand for Eph receptors, assumes a crucial role in orchestrating migration, repulsion, and adhesion during neuronal, vascular, and epithelial development. Functioning as a promiscuous binder, Ephrin-A1 engages Eph receptors on adjacent cells, facilitating contact-dependent bidirectional signaling. Its significance extends to angiogenesis and tumor neovascularization, where the recruitment of VAV2, VAV3, and the PI3-kinase p85 subunit by phosphorylated EPHA2 is pivotal for EFNA1-induced RAC1 GTPase activation, vascular endothelial cell migration, and assembly. Furthermore, Ephrin-A1 exerts anti-oncogenic effects by activating and down-regulating EPHA2, inducing its internalization and degradation. In the context of gliomas, Ephrin-A1 acts as a negative regulator, down-regulating EPHA2 and FAK, thereby mitigating the tumorigenesis process. Beyond its role in angiogenesis and tumorigenesis, Ephrin-A1 can elicit the collapse of embryonic neuronal growth cones and regulate dendritic spine morphogenesis. Existing as a monomer or homodimer, Ephrin-A1 forms heterodimers with EPHA2 and binds to a spectrum of receptor tyrosine kinases, including EPHA1, underscoring its diverse molecular interactions.