Background of the antigen
Ubiquitin is an abundant, highly conserved protein found in all eukaryotic cells either free or covalently attached to cellular proteins. 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). As an E2 class enzyme, UBE2W (Ubiquitin-conjugating enzyme E2 W), also known as Ubiquitin carrier protein W, is a 151 amino acid that catalyzes the conjugation of ubiquitin to proteins that are meant for lysosomal degradation. Functioning as a homodimer, UBE2W is widely expressed, with highest levels in testis. There are two isoforms of UBE2W that are produced as a result of alternative splicing events.