Human UCH-L3 / UCHL3 Protein, His Tag

N-6xHis, Unconjugated

-20°C

Powder

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.

Glu 2 - Ala 230

1.0 EU per μg

● -20°C to -70°C for 12 months in lyophilized state;
● -70°C for 3 months under sterile conditions after reconstitution._x000D_For long term storage, the product should be stored at lyophilized state at -20°C or lower.