Human UCH-L3 / UCHL3 Protein, His Tag | UC3-H5141-1mg

Human UCH-L3 / UCHL3 Protein, His Tag | UC3-H5141-1mg| Gentaur Distribution US, UK & Europe

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.

Source: Human UCH-L3, His Tag (UC3-H5141) is expressed from E. coli cells. It contains AA Glu 2 - Ala 230 (Accession # P15374-1).

Format: Powder.

Tag: N-6×His.

Expression System: E. coli.

Expression Region: Glu 2 - Ala 230.

Conjugate: Unconjugated.

Molecular Weight: 27.0 kDa.

Characteristics: 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).

Purity: 95%.

Buffer: 50 mM Tris, 150 mM NaCl, pH7.5.

Storage Conditions: -20℃.

Shipping Conditions: RT