UBE1L (E996) polyclonal antibody

The ubiquitin activating enzyme E1 (UBE1) catalyzes the first step in ubiquitin conjugation to mark cellular proteins for degradation. UBE1 activates ubiquitin by first adenylating (with ATP) its carboxy-terminal glycine residue and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ubiquitin-E1 thioester and a free AMP. UBE1 is an example of an X-Y homologous gene, which is X-linked with a distinct Y-linked gene in many mammals. UBE1L (Ubiquitin-activating enzyme E1 homolog), also known as UBA7 (Ubiquitin-like modifier-activating enzyme 7) or UBE2, is a 1011 amino acid homolog of UBE1. Like UBE1, UBE1L functions in the activation of ubiquitin through ATP-dependent adenylation. UBE1L is expressed in tumor cells and is a retinoid target that, through conjugation with ISG15 (Interferon-induced 15 kDa protein), triggers degradation and apoptosis in acute promyelocytic leukemia.