UCHL3 Mouse

Ubiquitin Carboxyl-Terminal Esterase L3 Mouse Recombinant
Cat. No.
BT19933
Source
Sf9, Baculovirus cells.
Synonyms
Ubiquitin carboxyl-terminal hydrolase isozyme L3, UCH-L3, UCHL3, Ubiquitin Carboxyl-Terminal Esterase L3, Ubiquitin thioesterase L3, Uchl3, Ubiquitin carboxyl-terminal esterase L3.
Appearance
Sterile Filtered clear solution.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Usage
Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

UCHL3 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 238 amino acids (1-230) and having a molecular mass of 27.2kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).
UCHL3 is fused to 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

Product Specs

Introduction
Ubiquitin carboxyl-terminal hydrolase isozyme L3, a member of a gene family responsible for hydrolyzing small C-terminal adducts of ubiquitin to generate the ubiquitin monomer, is known as UCHL3. This enzyme plays a crucial role in regulating neuronal development and spermatogenesis, and its dysfunction is linked to neurodegenerative diseases. Notably, UCHL3 shares a 54% homology with UCHL1.
Description
Produced in Sf9 Baculovirus cells, Recombinant Mouse UCHL3 is a single, glycosylated polypeptide chain. It consists of 238 amino acids (1-230) and has a molecular mass of 27.2kDa. Note that on SDS-PAGE, the molecular size will appear between 28-40kDa. The UCHL3 protein is fused to an 8 amino acid His-Tag at the C-terminus and purified using proprietary chromatographic techniques.
Physical Appearance
A clear solution that has been sterilized through filtration.
Formulation
The UCHL3 protein solution has a concentration of 0.5mg/ml. It is prepared in a buffer consisting of Phosphate buffered saline at a pH of 7.4 and contains 10% glycerol.
Stability
For short-term storage (2-4 weeks), keep the vial at 4°C. For longer storage, freeze at -20°C. Adding a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Avoid repeatedly freezing and thawing the solution.
Purity
The purity level is greater than 90.0% as determined by SDS-PAGE analysis.
Biological Activity
The specific activity is measured to be greater than 9,000 pmol/min/mg. This is defined as 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.
Synonyms
Ubiquitin carboxyl-terminal hydrolase isozyme L3, UCH-L3, UCHL3, Ubiquitin Carboxyl-Terminal Esterase L3, Ubiquitin thioesterase L3, Uchl3, Ubiquitin carboxyl-terminal esterase L3.
Source
Sf9, Baculovirus cells.
Amino Acid Sequence
MEGQRWLPLE ANPEVTNQFL KQLGLHPNWQ FVDVYGMEPE LLSMVPRPVC AVLLLFPITE KYEVFRTEEE EKIKSQGQDV TSSVYFMKQT ISNACGTIGL IHAIANNKDK MHFESGSTLK KFLEESVSMS PEERAKFLEN YDAIRVTHET SAHEGQTEAP SIDEKVDLHF IALVHVDGHL YELDGRKPFP INHGKTSDET LLEDAIEVCK KFMERDPDEL RFNAIALSAA LEHHHHHH.

Product Science Overview

Introduction

Ubiquitin Carboxyl-Terminal Esterase L3 (UCHL3) is a member of the ubiquitin C-terminal hydrolase family, which plays a crucial role in the ubiquitin-proteasome system. This system is essential for protein degradation and regulation within the cell. UCHL3 is a deubiquitinating enzyme (DUB) that specifically hydrolyzes the peptide bond at the C-terminal glycine of ubiquitin, releasing monomeric ubiquitin from ubiquitin-protein conjugates .

Gene and Protein Structure

The UCHL3 gene is located on chromosome 13q22.2 in humans and on a syntenic region on chromosome 14 in mice . The gene encodes a protein that is 230 amino acids in length with a predicted molecular weight of approximately 26 kDa . The protein contains a single N-terminal ubiquitin C-terminal hydrolase (UCH) domain, which is responsible for its enzymatic activity .

Expression and Function

UCHL3 is widely expressed in various tissues, with the highest levels observed in the heart, testis, thymus, and striated muscle . It is involved in several cellular processes, including the liberation of monomeric ubiquitin from precursors encoded by ubiquitin genes and the recycling of ubiquitin monomers . This activity is crucial for maintaining the balance of ubiquitin within the cell, which is necessary for proper protein degradation and regulation .

Biochemical Features

The crystal structure of human UCHL3 has been determined, revealing insights into its enzymatic mechanism . The protein’s active site contains a short crossover loop, which allows it to process small ubiquitin derivatives efficiently . Recombinant UCHL3 protein has been shown to display UCH activity in vitro, confirming its role as a deubiquitinating enzyme .

Animal Models and Research Applications

Studies involving mouse models have provided valuable insights into the function of UCHL3. Mice homozygous for a targeted deletion of the Uchl3 gene are indistinguishable from wild-type mice, suggesting that UCHL3 may have redundant functions with other deubiquitinating enzymes . However, double homozygous mice for both Uchl1 and Uchl3 genes display more severe phenotypes, including earlier onset of lethality and axonal degeneration .

Recombinant UCHL3 proteins, such as those derived from E. coli, are widely used in research to study the enzyme’s function and its role in various cellular processes . These recombinant proteins are typically supplied in a solution containing HEPES, NaCl, and TCEP, and are stored at -70°C to maintain stability .

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