UCHL3 Human
Description
UCHL3 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Product Science Overview
Ubiquitin Carboxyl-Terminal Esterase L3 (UCH-L3) is a member of the peptidase C12 family of deubiquitinating enzymes. It plays a crucial role in the ubiquitin-proteasome system, which is essential for protein degradation and regulation within the cell. This article delves into the structure, function, and significance of UCH-L3, particularly focusing on its human recombinant form.
UCH-L3 is a 230 amino acid protein with a predicted molecular weight of approximately 26.2 kDa . It is composed of a single N-terminal UCH domain, which includes a short active-site crossover loop. This structure allows UCH-L3 to process small ubiquitin derivatives efficiently . The human UCH-L3 shares 98% amino acid sequence identity with its mouse and rat orthologs .
UCH-L3 is involved in the processing of ubiquitin precursors and ubiquitinated proteins. It functions as a thiol protease, recognizing and hydrolyzing peptide bonds at the C-terminal glycine of ubiquitin or NEDD8 . This activity is crucial for the liberation of monomeric ubiquitin from precursors encoded by ubiquitin genes and for the recycling of ubiquitin monomers .
The human recombinant form of UCH-L3 is produced using E. coli expression systems. This recombinant protein is often used in research to study the enzyme’s function and to develop potential therapeutic applications. The recombinant UCH-L3 protein is typically supplied as a solution in HEPES, NaCl, and TCEP, and it is recommended to be stored at -70°C to maintain stability .
Recombinant UCH-L3 is used in various biochemical assays to understand its role in the ubiquitin-proteasome system. It is also employed in studies investigating the enzyme’s potential involvement in diseases where protein degradation is disrupted, such as neurodegenerative disorders and cancers.
