Human UCH-L3 / UCHL3 Protein, His Tag

Ubiquitin carboxyl-terminal hydrolase isozyme L3 (UCH-L3), a member of peptidase C12 family, is also known as ubiquitin thioesterase L3. Deubiquitinating enzyme (DUB) that controls levels of cellular ubiquitin through processing of ubiquitin precursors and ubiquitinated proteins. UCH-L3 is a thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of either ubiquitin or NEDD8. UCH-L3 indirectly increases the phosphorylation of IGFIR, AKT and FOXO1 and promotes insulin-signaling and insulin-induced adipogenesis. It is also required for stress-response retinal, skeletal muscle and germ cell maintenance. Furthermore, UCH-L3 may be involved in working memory and can hydrolyze UBB (+1), a mutated form of ubiquitin which is not effectively degraded by the proteasome and is associated with neurogenerative disorders.

This protein carries a polyhistidine tag at the N-terminus. The protein has a calculated MW of 27.0 kDa. The protein migrates as 28-30 kDa under reducing (R) condition (SDS-PAGE) .

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