GSTM5 Human, Active

Glutathione S-Transferase MU 5 Human Recombinant, Active
Cat. No.
BT7639
Source
E.coli.
Synonyms
Glutathione S-transferase mu 5, GSTM5-5, GST class-mu 5, GTM5, glutathione S-alkyltransferase M5, S-(hydroxyalkyl) glutathione lyase M5, EC 2.5.1.18.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 95% 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.
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Description

GSTM5 Human Recombinant produced in E. coli is a single polypeptide chain containing 242 amino acids (1-218) and having a molecular mass of 28.2 kDa.
GSTM5 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Glutathione S-transferase mu 5 (GSTM5) is a protein belonging to the glutathione s-transferase (GST) family. The GST family consists of eight classes: alpha, kappa, mu, omega, pi, sigma, theta, and zeta. Each class contains proteins with diverse cellular functions. GSTM5, a member of the mu class, plays a crucial role in detoxifying electrophilic compounds, such as carcinogens, drugs, environmental toxins, and oxidative stress products, by conjugating them with glutathione. GSTM5 is essential for detoxification processes, conjugating reduced glutathione to various exogenous and endogenous hydrophobic electrophiles.
Description
Recombinant human GSTM5, produced in E. coli, is a single polypeptide chain with a molecular weight of 28.2 kDa. It consists of 242 amino acids, including a 24 amino acid His-tag at the N-terminus (amino acids 1-218). Purification is achieved through proprietary chromatographic techniques.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
The GSTM5 solution is provided at a concentration of 1 mg/ml in a buffer containing 20mM Tris-HCl (pH 8.0), 0.1M NaCl, 1mM DTT, and 10% glycerol.
Stability
For short-term storage (2-4 weeks), keep the vial refrigerated at 4°C. For extended storage, freeze at -20°C. Adding a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Avoid repeated freeze-thaw cycles.
Purity
The purity is determined to be greater than 95% using SDS-PAGE analysis.
Biological Activity
The specific activity, a measure of the enzyme's ability to conjugate 1.0 µmole of 1-chloro-2,4-dinitrobenzene (CDNB) with reduced glutathione per minute at pH 6.5 and 25°C, is greater than 90,000 pmol/min/µg.
Synonyms
Glutathione S-transferase mu 5, GSTM5-5, GST class-mu 5, GTM5, glutathione S-alkyltransferase M5, S-(hydroxyalkyl) glutathione lyase M5, EC 2.5.1.18.
Source
E.coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMPMTLG YWDIRGLAHA IRLLLEYTDS SYVEKKYTLG DAPDYDRSQW LNEKFKLGLD FPNLPYLIDG AHKITQSNAI LRYIARKHNL CGETEEEKIR VDILENQVMD NHMELVRLCY DPDFEKLKPK YLEELPEKLK LYSEFLGKRP WFAGDKITFV DFLAYDVLDM KRIFEPKCLD AFLNLKDFIS RFEGLKKISA YMKSSQFLRG LLFGKSATWN SK.

Product Science Overview

Introduction

Glutathione S-Transferase Mu 5 (GSTM5) is an enzyme that belongs to the mu class of the glutathione S-transferase (GST) family. These enzymes play a crucial role in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress, by catalyzing their conjugation with glutathione .

Gene and Protein Structure

The GSTM5 gene is located on chromosome 1p13.3 and is part of a gene cluster that encodes the mu class of GST enzymes . The gene is highly polymorphic, meaning it has many genetic variations that can influence an individual’s susceptibility to carcinogens and toxins, as well as the toxicity and efficacy of certain drugs . The GSTM5 protein consists of 218 amino acids and has a molecular weight of approximately 25 kDa .

Function and Mechanism

GSTM5 functions by catalyzing the conjugation of reduced glutathione to a wide variety of hydrophobic and electrophilic compounds . This reaction is essential for the detoxification process, as it transforms harmful compounds into more water-soluble forms that can be easily excreted from the body . The enzyme’s activity is crucial in protecting cells from oxidative stress and maintaining cellular homeostasis .

Recombinant GSTM5

Recombinant human GSTM5 is produced using recombinant DNA technology, where the GSTM5 gene is cloned and expressed in a host organism, typically Escherichia coli . The recombinant enzyme retains its biological activity and is used in various research applications, including studies on detoxification mechanisms, drug metabolism, and the development of therapeutic agents .

Applications in Research

Recombinant GSTM5 is widely used in biochemical and pharmacological research. It serves as a model enzyme for studying the detoxification of electrophilic compounds and the role of GSTs in drug metabolism . Additionally, it is used in the development of assays to screen for potential inhibitors or activators of GST activity, which can have therapeutic implications for diseases related to oxidative stress and toxin exposure .

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GSTM5 Human
Glutathione S-Transferase MU 5 Human Recombinant
Cat. No.
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Source
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THE BIOTEK
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