Anti-UCHL3

In 1X PBS, pH 7.4, with 0.09% sodium azide. Covalent attachment of the C-terminus of ubiquitin to cellular proteins plays a role in a variety of cellular processes. Ubiquitin C-terminal hydrolysis is catalyzed by deubiquitinating (DUB) enzymes and is necessary for several functions, including liberation of monomeric ubiquitin from the precursors encoded by ubiquitin genes and recycling of ubiquitin monomers. There are 2 distinct families of DUBs, ubiquitin-specific proteases (UBPs) and ubiquitin C-terminal hydrolases (UCHs). Mayer and Wilkinson (1989) identified 4 distinct UCH activities from bovine thymus. All 4 were thiol proteases and had high-affinity binding sites for ubiquitin. Wilkinson et al. (1989) purified the predominant isozyme, UCHL3, and raised antibodies against it. By screening a human B-cell expression library with the antibodies, the authors isolated cDNAs encoding human UCHL3. Sequence comparisons revealed that the sequence of the predicted 230-amino acid human UCHL3 protein is 54% identical to that of UCHL1. Protein function: Deubiquitinating enzyme (DUB) that controls levels of cellular ubiquitin through processing of ubiquitin precursors and ubiquitinated proteins. Thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of either ubiquitin or NEDD8. Has a 10-fold preference for Arg and Lys at position P3", and exhibits a preference towards 'Lys-48'-linked Ubiquitin chains. Deubiquitinates ENAC in apical compartments, thereby regulating apical membrane recycling. Indirectly increases the phosphorylation of IGFIR, AKT and FOXO1 and promotes insulin- signaling and insulin-induced adipogenesis. Required for stress- response retinal, skeletal muscle and germ cell maintenance. May be involved in working memory. Can hydrolyze UBB(+1), a mutated form of ubiquitin which is not effectively degraded by the proteasome and is associated with neurogenerative disorders. [The UniProt Consortium]