USP11 Rabbit anti-Human, Polyclonal, Proteintech

Description

• Modification of target proteins by ubiquitin participates in a wide array of biological functions
• Proteins destined for degradation or processing via the 26 S proteasome are coupled to multiple copies of ubiquitin
• However, attachment of ubiquitin or ubiquitin-related molecules may also result in changes in subcellular distribution or modification of protein activity
• An additional level of ubiquitin regulation, deubiquitination, is catalyzed by proteases called deubiquitinating enzymes, which fall into four distinct families
• Ubiquitin C-terminal hydrolases, ubiquitin-specific processing proteases (USPs),1 OTU-domain ubiquitin-aldehyde-binding proteins, and Jab1/Pad1/MPN-domain-containing metallo-enzymes
• Among these four families, USPs represent the most widespread and represented deubiquitinating enzymes across evolution
• USPs tend to release ubiquitin from a conjugated protein
• They display similar catalytic domains containing conserved Cys and His boxes but divergent N-terminal and occasionally C-terminal extensions, which are thought to function in substrate recognition, subcellular localization, and protein-protein interactions.