Uchl3
Origine: Humain
Hôte: Escherichia coli (E. coli)
Recombinant
> 97 % as determined by reducing SDS-PAGE.
Active
Indications d'application
This recombinant protein can be used for WB.
Restrictions
For Research Use only
Format
Lyophilized
Buffer
50 mM Tris, 150 mM NaCl, pH 7.5
Conseil sur la manipulation
Avoid repeated freeze-thaw cycles.
Stock
-20 °C,-80 °C
Stockage commentaire
Lyophilized Protein should be stored at -20°C or lower for long term storage. Upon reconstitution, working aliquots should be stored at -20°C or -70°C.
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.