UCHL1 Mouse

Source: Escherichia Coli.Sterile Filtered colorless solution.Ubiquitin Carboxyl-Terminal Esterase L1 (UCHL1) is a part of a family whose products hydrolyze small C-terminal adducts of ubiquitin to create the ubiquitin monomer. UCHL1 is a part of the ubiquitin system, which regulates many biological activities. UCHL1 is a thiol protease that distinguishes and hydrolyzes a peptide bond at the C-terminal glycine of ubiquitin. UCHL1 binds to free monoubiquitin and avoids its degradation in lysosomes.UCHL1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 246 amino acids (1-223a.a) and having a molecular mass of 27.2kDa. UCHL1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques. Protein function: Ubiquitin-protein hydrolase involved both in the processing of ubiquitin precursors and of ubiquitinated proteins (Probable). This enzyme is a thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of ubiquitin (PubMed:12913066). Also binds to free monoubiquitin and may prevent its degradation in lysosomes (PubMed:12913066). The homodimer may have ATP-independent ubiquitin ligase activity. [The UniProt Consortium]