Ubiquitin vinyl sulfone (human) (rec.)

Ubiquitin is a small (8.5kDa) regulatory protein that has been found in almost all tissues of eukaryotic organisms. The addition of ubiquitin to a substrate protein is called ubiquitination or ubiquitylation. Ubiquitination can affect proteins in many ways: it can signal for their degradation via the proteasome, alter their cellular location, affect their activity and promote or prevent protein interactions. Removal of ubiquitin from a substrate protein occurs via deconjugating enzymes, of which there are nearly 100 known enzymes with various linkage specificities. This product consists of a full-length human, mature ubiquitin polypeptide (amino acids 1-76), expressed in E.coli with a C-terminal warhead (Vinyl Sulfone). Ubiquitin vinyl sulfone is a potent, irreversible and specific inhibitor of deubiquitinating enzymes (DUBs) based on a C-terminal electrophilic vinyl sulfone group. Ubiquitin vinyl sulfone can be used for activity profiling experiments and determining DUB inhibitor specificity. It targets four of the five major DUB families: UCH (Ubiquitin C-terminal hydrolases), USP (Ubiquitin specific proteases), OTU (Ovarian tumor proteases) and MJD (Machado-Josephin domain proteases) while JAMM metalloproteases are not inhibited.