Human UCH-L3 / UCHL3 Protein

• Catalog Number: orb348793
• Category: Proteins
• Description: 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.
• Reactivity: Human
• Tag: N-6×His
• Form/Appearance: Powder
• Purity: 95%
• Conjugation: Unconjugated
• MW: 27.0 kDa
• Target: UCH-L3
• Protein Sequence: AAH18125.1
• Source: Human UCH-L3, His Tag (orb348793) is expressed from E. coli cells. It contains AA Glu 2 - Ala 230 (Accession # P15374-1).
• Expression System: E. coli
• Expression Region: Glu 2 - Ala 230
• Endotoxins: 1.0 EU per μg
• NCBI: AAH18125.1
• Storage: -20℃
• Buffer/Preservatives: 50 mM Tris, 150 mM NaCl, pH7.5
• Alternative names: UCHL3,Ubiquitin thioesterase L3
• Note: For research use only
• Application notes: 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).
• Expiration Date: 6 months from date of receipt.

SDS-PAGE analysis of Human UCH-L3 protein