Catalog number: SBB-DE0023, 50 μg
UCHL3 is a deubiquitinating enzyme (DUB) that controls levels of cellular ubiquitin through processing of ubiquitin precursors and ubiquitinated proteins. It is a thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of either ubiquitin or NEDD8. It digests precursors and ubiquitinated proteins to generate monomeric ubiquitin. This UCHL3 is recombinatly expressed in E.coli.[1][2][3][4][5]
UCHL3, human recombinant
UCHL3 (Ubiquitin C-terminal Hydrolase L3) is a deubiquitinating enzyme (DUB) that controls levels of cellular ubiquitin through processing of ubiquitin precursors and ubiquitinated proteins. It is a thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of either ubiquitin or NEDD8. It plays a role in regulating apical membrane recycling, and indirectly increases the phosphorylation of IGFIR, AKT and FOXO1 and promotes insulin-signaling and insulin-induced adipogenesis. It is required for stress-response in retinal, skeletal muscle and germ cell maintenance. UCHL3 is also known to hydrolyze UBB(+1), a mutated form of ubiquitin which is not effectively degraded by the proteasome and is associated with neurogenerative disorders. It digests precursors and ubiquitinated proteins to generate monomeric ubiquitin. This UCHL3 is recombinatly expressed in E.coli.