This is a synthetic peptide designed for use in combination with anti-Uchl3 Antibody. It may block above mentioned antibody from binding to its target protein in western blot and/or immunohistochecmistry under proper experimental settings. There is no guarantee for its use in other applications.
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. Uchl3 has a 10-fold preference for Arg and Lys at position P3', and exhibits a preference towards 'Lys-48'-linked Ubiquitin chains. Uchl3 deubiquitinates ENAC in apical compartments, thereby regulating apical membrane recycling. Uchl3 indirectly increases the phosphorylation of IGFIR, AKT and FOXO1 and promotes insulin-signaling and insulin-induced adipogenesis. It is required for stress-response retinal, skeletal muscle and germ cell maintenance. Uchl3 may be involved in working memory and can hydrolyze UBB(+1), a mutated form of ubiquitin which is not effectively degraded by the proteasome.