Anti-COPI coat complex subunit epsilon antibodies are used for the immunodetection of the protein encoded by the COPE gene. In humans, the canonical protein has a reported length of 308 amino acid residues and a mass of 34.5 kDa. Its subcellular localization is in the membrane, cytoplasmic vesicles, Golgi, and cytoplasm. Alternative splicing is reported to yield 3 different isoforms for this protein. A member of the COPE protein family, it is known to be involved with Golgi transport and protein transport. Post-translational modifications have been described, including ubiquitination and phosphorylation. Other names for this target antigen include coatomer subunit epsilon, coatomer epsilon subunit, coatomer protein complex subunit epsilon, epsilon coat protein, and epsilon-COP. Gene orthologs have been identified in the mouse, rat, bovine, frog, zebrafish, chimpanzee and chicken species.