GSTM2 Human

Glutathione S-Transferase MU 2 Human Recombinant
Cat. No.
BT7228
Source
Escherichia Coli.
Synonyms
Glutathione S-transferase Mu 2, GST class-mu 2, GSTM2-2, GSTM2, GST4, GSTM, GTHMUS, MGC117303.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 95.0% 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

GSTM2 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 238 amino acids (1-218 a.a.) and having a molecular mass of 27.9kDa. The GSTM2 is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Glutathione S-transferase Mu 2 (GSTM2) is a member of the glutathione s-transferase (GST) protein family. These enzymes play a crucial role in detoxification by catalyzing the conjugation of glutathione with electrophilic compounds, including carcinogens, drugs, toxins, and oxidative stress byproducts. GSTM2, belonging to the mu class, is one of eight GST families (alpha, kappa, mu, omega, pi, sigma, theta, zeta). Genes encoding the mu class enzymes are located on chromosome 1p13.3 and exhibit high polymorphism. This genetic variation influences individual susceptibility to carcinogens and toxins, impacting the toxicity and efficacy of certain drugs.
Description
Recombinant human GSTM2, expressed in E. coli, is a purified protein with a His tag. This non-glycosylated polypeptide chain comprises 238 amino acids (with the His tag at the N-terminus) and has a molecular weight of 27.9kDa. The purification process employs proprietary chromatographic techniques.
Physical Appearance
Clear, colorless solution that has been sterilized by filtration.
Formulation
The GSTM2 solution is supplied at a concentration of 0.5mg/ml in a buffer consisting of 20mM Tris-HCl (pH 8.0), 10% glycerol, 0.1M NaCl, and 1mM DTT.
Stability
For short-term storage (2-4 weeks), the GSTM2 solution can be kept at 4°C. For extended storage, freeze the solution at -20°C. Adding a carrier protein like HSA or BSA (0.1%) is recommended for long-term storage. Minimize repeated freeze-thaw cycles.
Purity
The purity of GSTM2 is greater than 95% as assessed by SDS-PAGE analysis.
Biological Activity
GSTM2 exhibits a specific activity of less than 25 units/mg. One unit of activity refers to the enzyme's ability to conjugate 1.0 µmole of 1-chloro-2,4-dinitrobenzene (CDNB) with reduced glutathione per minute at a pH of 6.5 and a temperature of 25°C.
Synonyms
Glutathione S-transferase Mu 2, GST class-mu 2, GSTM2-2, GSTM2, GST4, GSTM, GTHMUS, MGC117303.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MPMTLGYWNI RGLAHSIRLL LEYTDSSYEE KKYTMGDAPD YDRSQWLNEK FKLGLDFPNL PYLIDGTHKI TQSNAILRYI ARKHNLCGES EKEQIREDIL ENQFMDSRMQ LAKLCYDPDF EKLKPEYLQA LPEMLKLYSQ FLGKQPWFLG DKITFVDFIA YDVLERNQVF EPSCLDAFPN LKDFISRFEG LEKISAYMKS SRFLPRPVFT KMAVWGNK.

Product Science Overview

Introduction

Glutathione S-Transferase Mu 2 (GSTM2) is a member of the glutathione S-transferase (GST) family, which plays a crucial role in the detoxification of endogenous and exogenous compounds. GSTM2 is involved in the conjugation of reduced glutathione to a wide variety of hydrophobic and electrophilic compounds, facilitating their excretion from the body.

Structure and Function

GSTM2 is a protein-coding gene that encodes for the enzyme glutathione S-transferase Mu 2. This enzyme is part of the larger GST superfamily, which is divided into several classes, including Alpha, Mu, Pi, and Theta. The Mu class, to which GSTM2 belongs, is characterized by its ability to conjugate glutathione to a variety of substrates, including carcinogens, therapeutic drugs, and products of oxidative stress .

The primary function of GSTM2 is to catalyze the conjugation of glutathione to electrophilic compounds, thereby neutralizing their reactivity and facilitating their excretion. This process is essential for cellular detoxification and protection against oxidative stress. GSTM2 is also involved in the metabolism of various xenobiotics and endogenous compounds, contributing to the overall detoxification capacity of the cell .

Biological Significance

GSTM2 plays a significant role in protecting cells from oxidative damage and maintaining cellular homeostasis. It is expressed in various tissues, including the liver, where it contributes to the detoxification of harmful compounds. The enzyme’s activity is crucial for the metabolism of drugs and the detoxification of reactive oxygen species (ROS), which can cause cellular damage if not properly managed .

In addition to its detoxification role, GSTM2 has been implicated in various diseases. For instance, alterations in GSTM2 expression have been associated with an increased risk of certain cancers, including colon adenocarcinoma . The enzyme’s role in detoxifying carcinogens suggests that it may have a protective effect against cancer development. Furthermore, GSTM2 has been linked to other conditions, such as autism spectrum disorder and cranioectodermal dysplasia .

Clinical Applications

Recombinant human GSTM2 has been utilized in various research and clinical applications. The recombinant form of the enzyme is produced using genetic engineering techniques, allowing for the study of its structure, function, and potential therapeutic uses. Recombinant GSTM2 is often used in biochemical assays to investigate its role in detoxification processes and its interactions with other molecules .

In clinical research, GSTM2 has been studied for its potential as a biomarker for certain diseases. For example, changes in GSTM2 expression levels have been investigated as potential indicators of cancer risk and progression . Additionally, the enzyme’s role in drug metabolism makes it a target for studying drug interactions and potential adverse effects.

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