GSTM1 Mouse

Glutathione S-Transferase M1 Mouse Recombinant
Cat. No.
BT7073
Source
Escherichia Coli.
Synonyms
GST1, GTH4, GTM1, GSTM1-1, MGC26563, GSTM1a-1a, GSTM1b-1b, GSTM1, Glutathione S-transferase Mu 1, GST class-mu 1, Glutathione S-transferase GT8.7, pmGT10, GST 1-1.
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

GSTM1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 218 amino acids and having a molecular mass of 25.9 kDa.
The GTM1 is purified by proprietary chromatographic techniques.

Product Specs

Introduction
The soluble cytoplasmic mammalian GSTs are divided into eight classes: alpha, kappa, mu, omega, pi, sigma, theta, and zeta. Two different supergene families encode cytosolic and membrane-bound GST types. The detoxification of electrophilic compounds, such as carcinogens, therapeutic medications, environmental toxins, and oxidative stress products, by conjugation with glutathione, is carried out by the mu class of enzymes. On chromosome 1p13.3, a gene cluster containing the genes that code for the mu class of enzymes is highly polymorphic. These genetic variations may affect an individual's susceptibility to toxins and carcinogens and the effectiveness and toxicity of some medications. The development of several cancers has been linked to null mutations in this mu class gene.
Description
GSTM1 Mouse Recombinant is a single, non-glycosylated polypeptide chain with a molecular weight of 25.9 kDa that contains 218 amino acids. It is produced in E. coli. Proprietary chromatographic methods are used to purify the GTM1.
Physical Appearance
Colorless solution that has been sterile filtered.
Formulation
PBS pH-7.4 and 5mM glutathione are present in the GSTM1 solution.
Stability
Store at 4°C for 2-4 weeks if the entire vial will be used. It is advised to add a carrier protein (0.1% HSA or BSA) for long-term storage. For extended storage, keep frozen at -20°C. Avoid repeated freeze-thaw cycles.
Purity
Greater than 95.0% as determined by SDS-PAGE analysis.
Biological Activity
The specific activity, which is measured at pH 6.5 and 25°C, is 3 units/mg. It is defined as the quantity of enzyme that conjugates 1.0 umole of 1-chloro-2,4-dinitrobenzene (CDNB) with reduced glutathione per minute.
Synonyms
GST1, GTH4, GTM1, GSTM1-1, MGC26563, GSTM1a-1a, GSTM1b-1b, GSTM1, Glutathione S-transferase Mu 1, GST class-mu 1, Glutathione S-transferase GT8.7, pmGT10, GST 1-1.
Source
Escherichia Coli.
Amino Acid Sequence
MPMILGYWNV RGLTHPIRML LEYTDSSYDE KRYTMGDAPD FDRSQWLNEK FKLGLDFPNL PYLIDGSHKI TQSNAILRYL ARKHHLDGET EEERIRADIV ENQVMDTRMQ LIMLCYNPDF EKQKPEFLKT IPEKMKLYSE FLGKRPWFAG DKVTYVDFLA YDILDQYRMF EPKCLDAFPN LRDFLARFEG LKKISAYMKS SRYIATPIFS KMAHWSNK.

Product Science Overview

Introduction

Glutathione S-Transferase M1 (GSTM1) is a member of the glutathione S-transferase (GST) family, which plays a crucial role in detoxification processes. GSTs are enzymes that catalyze the conjugation of the antioxidant molecule glutathione (GSH) to various endogenous and exogenous electrophilic compounds. This process is essential for the detoxification of harmful substances and the protection of cellular components from oxidative damage.

Structure and Function

GSTM1 is a phase II detoxification enzyme predominantly expressed in the liver. It is involved in the metabolism of a wide range of substrates, including carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress. The enzyme’s activity is crucial for maintaining cellular homeostasis and protecting against cellular damage.

The structure of GSTM1 includes a highly conserved GSH-binding site and a more variable substrate-binding site. This dual binding capability allows GSTM1 to interact with a diverse array of substrates, making it a versatile enzyme in detoxification pathways.

Recombinant Expression

Recombinant GSTM1 (Mouse) is produced using Escherichia coli expression systems. The recombinant protein is typically purified to a high degree of purity (>95%) and is suitable for various biochemical assays, including SDS-PAGE. The availability of recombinant GSTM1 allows for detailed studies on its enzymatic properties, substrate specificity, and potential applications in biotechnology and medicine .

Biological Significance

GSTM1 plays a significant role in protecting cells from oxidative stress and toxic insults. It is involved in the detoxification of reactive oxygen species (ROS) and the metabolism of xenobiotics. The enzyme’s activity is particularly important in the liver, where it helps to neutralize harmful compounds and prevent liver damage.

Research has shown that GSTM1 is upregulated in response to chronic alcohol consumption, providing a protective mechanism against alcohol-induced liver injury. The enzyme counteracts the activation of apoptosis signal-regulating kinase 1 (ASK1) and its downstream signaling pathways, thereby mitigating oxidative stress and inflammation in the liver .

Applications in Research and Medicine

Recombinant GSTM1 is widely used in research to study its role in detoxification processes and its potential therapeutic applications. The enzyme’s ability to neutralize harmful compounds makes it a valuable tool in the development of treatments for diseases associated with oxidative stress and toxin exposure.

In addition, GSTM1 has potential applications in biotechnology, such as the development of biosensors for detecting environmental toxins and the engineering of plants with enhanced resistance to biotic and abiotic stresses .

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