epitope mapping at the N-terminus of UBE2H of human origin
recommended for detection of UBE2H of mouse, rat and human origin by WB, IF and ELISA; non cross-reactive with other UBE2 family members; also reactive with additional species, including equine, canine, bovine, porcine and avian
UBE2H Background Information UBE2H (ubiquitin-conjugating enzyme E2H), also known as UBC8, UBCH, UBCH2 or E2-20K, is a 183 amino acid protein involved in ubiquitin-mediated protein degradation. Ubiquitination is an important mechanism through which three classes of enzymes act in concert to target short-lived or abnormal proteins for destruction. The three classes of enzymes involved in ubiquitination are the ubiquitin-activating enzymes (E1s), the ubiquitin-conjugating enzymes (E2s) and the ubiquitin-protein ligases (E3s). One of several members of the ubiquitin-conjugating enzyme family, UBE2H functions as an E2 ubiquitin-conjugating enzyme that acts to catalyze the covalent attachment of ubiquitin residues to various proteins, including Histone H2A. UBE2H shares 100% identity with its mouse counterpart and 98% identity with its frog and zebrafish homologs, suggesting a conserved function between species. Multiple isoforms of UBE2H exist due to alternative splicing events.
