GSTM5 Human

Glutathione S-Transferase MU 5 Human Recombinant
Cat. No.
BT7533
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.
Shipped with Ice Packs
In Stock

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. GST proteins are categorized into eight families: alpha, kappa, mu, omega, pi, sigma, theta, and zeta. Each family contains proteins with diverse cellular functions. As a member of the mu class, GSTM5 plays a crucial role in detoxification by conjugating glutathione to various electrophilic compounds, including carcinogens, drugs, environmental toxins, and oxidative stress byproducts. GSTM5 is essential for detoxification, conjugating reduced glutathione to a wide range of 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 (1-218) and is fused to a 24 amino acid His-tag at the N-terminus. Purification is achieved through proprietary chromatographic techniques.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
GSTM5 is supplied as a 1 mg/ml solution in a buffer consisting of 20mM Tris-HCl (pH 8.0), 0.1M NaCl, 1mM DTT, and 10% glycerol.
Stability
For short-term storage (up to 4 weeks), the product can be stored at 4°C. For extended storage, it is recommended to freeze the product at -20°C. The addition of a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Avoid repeated freeze-thaw cycles.
Purity
The purity of GSTM5 is greater than 95% as determined by SDS-PAGE analysis.
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

Structure and Function

GSTM5 is a cytosolic enzyme that catalyzes the conjugation of reduced glutathione to a wide variety of hydrophobic and electrophilic compounds. This process is essential for the detoxification and elimination of harmful substances from the body . The enzyme is composed of 242 amino acids and has a molecular mass of approximately 28.2 kDa .

Genetic and Biochemical Properties

The GSTM5 gene is located on chromosome 1p13.3 and is part of a gene cluster that includes other members of the mu class of GSTs . These genes are highly polymorphic, meaning they exhibit a high degree of genetic variation. This polymorphism can influence an individual’s susceptibility to carcinogens and toxins, as well as the toxicity and efficacy of certain drugs .

Expression and Regulation

GSTM5 is expressed in various tissues, including the liver, where it plays a significant role in detoxification processes. The expression of GSTM5 can be regulated by various factors, including oxidative stress and exposure to xenobiotics (foreign chemical substances) .

Applications in Research and Medicine

Recombinant human GSTM5 is produced using techniques such as expression in E. coli, allowing for the study of its biochemical properties and potential therapeutic applications . The enzyme is used in research to understand its role in detoxification and its potential implications in diseases such as cancer .

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