UCHL1 Mouse, Active
Description
UCHL1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 246 amino acids (1-223 a.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.
Product Specs
Ubiquitin Carboxyl-Terminal Esterase L1 (UCHL1) is a member of a family of enzymes that hydrolyze small C-terminal adducts of ubiquitin, resulting in the formation of ubiquitin monomers. UCHL1 plays a crucial role in the ubiquitin system, which is responsible for regulating various biological processes. As a thiol protease, UCHL1 specifically recognizes and cleaves a peptide bond located at the C-terminal glycine residue of ubiquitin. Additionally, UCHL1 exhibits binding affinity for free monoubiquitin, thereby preventing its degradation within lysosomes.
Recombinant UCHL1 from mouse, expressed in E. coli, is a single, non-glycosylated polypeptide chain composed of 246 amino acids (specifically, amino acids 1-223). This protein has a molecular weight of 27.2 kDa. The N-terminus of UCHL1 is fused to a 23 amino acid His-tag. Purification is achieved through proprietary chromatographic methods.
The product appears as a sterile, colorless solution after filtration.
The UCHL1 protein solution is provided at a concentration of 1 mg/ml and is formulated in a buffer consisting of Phosphate buffered saline (pH 7.4), 10% glycerol, and 1mM DTT.
For short-term storage (up to 2-4 weeks), the product should be kept at 4°C. For extended storage, it is recommended to freeze the product at -20°C. To ensure optimal long-term stability, adding a carrier protein like HSA or BSA (0.1%) is advisable. Repeated freezing and thawing cycles should be minimized.
The purity of the product is greater than 90% as determined by SDS-PAGE analysis.
The specific activity of the enzyme is measured to be greater than 70 pmol/min/ug. Specific activity represents the amount of enzyme required to hydrolyze 1.0 pmole of ubiquitin-AMC per minute at a pH of 7.5 and a temperature of 37°C.
MGSSHHHHHH SSGLVPRGSH MGSMQLKPME INPEMLNKVL AKLGVAGQWR FADVLGLEEE TLGSVPSPAC ALLLLFPLTA QHENFRKKQI EELKGQEVSP KVYFMKQTIG NSCGTIGLIH AVANNQDKLE FEDGSVLKQF LSETEKLSPE DRAKCFEKNE AIQAAHDSVA QEGQCRVDDK VNFHFILFNN VDGHLYELDG RMPFPVNHGA SSEDSLLQDA AKVCREFTER EQGEVRFSAV ALCKAA.
Product Science Overview
UCHL1 is one of the most abundant proteins in the brain, constituting 1-2% of the total soluble protein . It has hydrolase activities in the ubiquitin-proteasome pathway and, in vitro studies, have also shown ubiquitin ligase activity . The enzyme recognizes and hydrolyzes a peptide bond at the C-terminal glycine of ubiquitin to maintain a stable pool of monoubiquitin, which is essential for the ubiquitin-proteasome and autophagy-lysosome pathways .
UCHL1 plays a significant role in various biological processes, including:
- Maintenance of Synaptic Function: It is involved in the regulation of synaptic function, which is crucial for neuronal communication .
- Cardiac Function: UCHL1 has been implicated in the regulation of cardiac function .
- Inflammatory Response: It plays a role in modulating the inflammatory response .
- Osteoclastogenesis: UCHL1 regulates the process of osteoclastogenesis, which is the formation of osteoclasts involved in bone resorption .
Mutations in the UCHL1 gene have been associated with neurodegenerative disorders. For instance, recessive loss of function of UCHL1 has been implicated in early-onset progressive neurodegeneration . Studies have shown that different mutations in UCHL1 can lead to varying functional consequences, such as increased enzyme activity or loss of function .
Recombinant UCHL1 (Mouse) is widely used in research to study its enzymatic activity and role in various biological processes. The recombinant form is particularly useful for in vitro studies to understand the enzyme’s function and its implications in diseases.
