Recombinant Human EphA10 Fc Chimera Protein, CF

EphA10 is a member of the transmembrane Eph receptor tyrosine kinase family. Although the A and B classes of Eph proteins have a common structural organization, they are distinguished by their preference for Ephrin ligands. Eph-Ephrin interactions are widely involved in the regulation of cell migration, tissue morphogenesis, and cancer progression (1-4). The 532 amino acid (aa) extracellular domain (ECD) of human EphA10 contains an N-terminal Ephrin binding region followed by two fibronectin type II domains, a 422 aa cytoplasmic domain contains the tyrosine kinase domain and a sterile alpha motif (SAM) (5). Alternate splicing generates a soluble isoform that is truncated following the Ephrin binding region, and a transmembrane isoform that lacks only the SAM (5). Within the ECD, human EphA10 shares 38%-54% aa sequence identity with other EphA and EphB proteins. It shares 95% and 88% aa sequence identity with the ECD of mouse and rat EphA10, respectively. EphA10 is preferentially expressed in testis and is upregulated in some breast and prostate carcinoma cell lines (5- 7). It selectivity binds Ephrin-A1, 2, 3, 4,and 5 relative to Ephrin-B1 and -B2 (5).