UCHL1 Mouse

Ubiquitin Carboxyl-Terminal Esterase L1 Mouse Recombinant
Cat. No.
BT23542
Source
Escherichia Coli.
Synonyms
Ubiquitin carboxyl-terminal hydrolase isozyme L1, UCH-L1, Neuron cytoplasmic protein 9.5, PGP 9.5, PGP9.5, Ubiquitin thioesterase L1.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

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.

Product Specs

Introduction
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. This enzyme plays a crucial role in the ubiquitin system, which is responsible for regulating a wide range of biological processes. UCHL1 functions as a thiol protease, specifically recognizing and cleaving the peptide bond at the C-terminal glycine residue of ubiquitin. Additionally, UCHL1 binds to free monoubiquitin, thereby preventing its degradation within lysosomes.
Description
Recombinant UCHL1 from mouse has been produced in E. coli. This non-glycosylated polypeptide chain consists of 246 amino acids (residues 1-223a.a) and has a molecular weight of 27.2 kDa. The protein includes a 23 amino acid His-tag fused at the N-terminus. Purification is achieved through proprietary chromatographic techniques.
Physical Appearance
Clear, colorless solution that has been sterilized by filtration.
Formulation
The UCHL1 protein solution is provided at a concentration of 1 mg/ml and is formulated in a buffer consisting of phosphate-buffered saline (PBS), 10% glycerol, and 1 mM DTT.
Stability
For short-term storage (2-4 weeks), the product can be stored at 4°C. For extended storage, it is recommended to freeze the product at -20°C. To ensure optimal long-term stability, the addition of a carrier protein such as HSA or BSA (0.1%) is advised. Multiple freeze-thaw cycles should be avoided.
Purity
The purity of the product is greater than 90.0%, as determined by SDS-PAGE analysis.
Synonyms
Ubiquitin carboxyl-terminal hydrolase isozyme L1, UCH-L1, Neuron cytoplasmic protein 9.5, PGP 9.5, PGP9.5, Ubiquitin thioesterase L1.
Source
Escherichia Coli.
Amino Acid Sequence
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

Structure and Function

UCHL1 is a thiol protease that hydrolyzes a peptide bond at the C-terminal glycine of ubiquitin . This enzyme plays a crucial role in the ubiquitin-proteasome pathway, which is responsible for degrading unneeded or damaged proteins by tagging them with ubiquitin . The enzyme’s hydrolase activity helps in processing ubiquitin precursors and recycling ubiquitin from ubiquitin-protein conjugates .

Expression and Localization

UCHL1 constitutes about 1-2% of the total soluble protein in the brain, making it one of the most abundant proteins in this organ . It is specifically expressed in neurons and is involved in maintaining neuronal health and function . The enzyme is also found in cells of the diffuse neuroendocrine system, which includes various hormone-producing cells scattered throughout the body .

Recombinant UCHL1

Recombinant UCHL1, such as the mouse recombinant version, is produced using genetic engineering techniques. This involves inserting the UCHL1 gene into a suitable expression system, such as bacteria or mammalian cells, to produce the protein in large quantities . Recombinant proteins are used in various research applications, including studying the enzyme’s structure, function, and role in diseases .

Role in Disease

Mutations in the UCHL1 gene have been associated with several neurodegenerative disorders, including Parkinson’s disease . These mutations can lead to either loss of function or gain of function of the enzyme, affecting its ability to process ubiquitin and maintain protein homeostasis . For example, certain mutations can increase the enzyme’s hydrolytic activity, while others can render the enzyme insoluble and inactive .

Research and Applications

UCHL1 is a subject of extensive research due to its critical role in the nervous system and its association with neurodegenerative diseases . Studies on recombinant UCHL1 help in understanding the enzyme’s function, identifying potential therapeutic targets, and developing treatments for related disorders . Additionally, UCHL1 is used as a neuronal marker in various experimental settings due to its high expression in neurons .

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