Purity ~95% (SDS-PAGE). EphA7, also known as Mdk1, Hek11, Ehk3, Ebk, and Cek11, is a 115-120kD glycosylated member of the Eph family of transmembrane receptor tyrosine kinases. The A and B classes of Eph proteins are distinguished by Ephrin ligand binding preference but have a common structural organization. EphA7 preferentially binds to and is activated by Ephrin-A1, -A2, -A3, -A4, and -A5. Eph-Ephrin interactions are widely involved in the regulation of cell migration, tissue morphogenesis, and cancer progression. The 532aa extracellular domain (ECD) of human EphA7 contains an N-terminal Ephrin binding region, a cysteine-rich region, and two fibronectin type III domains (FnIII). The 421aa cytoplasmic domain contains the tyrosine kinase domain and a sterile alpha motif (SAM). Within the ECD, human EphA7 shares 98% aa sequence identity with mouse and rat EphA7. Alternate splicing generates secreted isoforms of human EphA7 that are truncated either before or following the first FnIII do