UCHL3, Ubiquitin thioesterase L3
Human UCH-L3 / UCHL3 Protein (Human UCH-L3, His Tag) Glu 2 - Ala 230 (Accession # AAH18125) was produced in E.coli cells at ACROBiosystems.
Human UCH-L3, His Tag is fused with a polyhistidine tag at the N-terminus, and has a calculated MW of 27 kDa. The predicted N-terminus is Met. The reducing (R) protein migrates as 27 kDa in SDS-PAGE .
Less than 1.0 EU per μg by the LAL method.
>95% as determined by SDS-PAGE.
Lyophilized from 0.22 μm filtered solution in 50 mM tris, 150 mM NaCl, pH7.5. Normally Trehalose are added as protectants before lyophilization.
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See Certificate of Analysis for reconstitution instructions and specific concentrations.
Avoid repeated freeze-thaw cycles.
No activity loss was observed after storage at:
In lyophilized state for 1 year (4°C); After reconstitution under sterile conditions for 3 months (-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.
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