GSTM4 Human

Glutathione S-Transferase MU 4 Human Recombinant
Cat. No.
BT7389
Source
Escherichia Coli.
Synonyms
Glutathione S-transferase Mu 4, EC=2.5.1.18, GST class-mu 4, GST-Mu2, GSTM4-4, GSTM4, GTM4, GSTM4-4, MGC9247, MGC131945.
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

GSTM4 Recombinant Human 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 27.7 kDa. The GSTM4 is fused to a 20 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Product Specs

Introduction
GSTM4, a member of the glutathione s-transferase (GST) family, plays a crucial role in cellular detoxification. GST proteins are categorized into eight families (alpha, kappa, mu, omega, pi, sigma, theta, and zeta), each with diverse functions. GSTM4, belonging to the mu class, specializes in detoxifying electrophilic compounds, including carcinogens, drugs, environmental toxins, and oxidative stress products, by conjugating them with glutathione.
Description
Recombinant Human GSTM4, produced in E. coli, is a non-glycosylated polypeptide chain consisting of 238 amino acids (1-218 a.a.). With a molecular weight of 27.7 kDa, it features a 20 amino acid His-Tag fused at the N-terminus. Purification is achieved using proprietary chromatographic techniques.
Physical Appearance
Clear, colorless solution, sterilized by filtration.
Formulation
GSTM4 Human solution in a buffer composed of 20mM Tris-HCl (pH 8), 1mM DTT, 0.05M NaCl, and 10% glycerol.
Stability
For short-term storage (2-4 weeks), refrigerate at 4°C. For extended periods, freeze at -20°C. Adding a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Minimize freeze-thaw cycles.
Purity
Purity exceeds 95.0% as determined by SDS-PAGE analysis.
Synonyms
Glutathione S-transferase Mu 4, EC=2.5.1.18, GST class-mu 4, GST-Mu2, GSTM4-4, GSTM4, GTM4, GSTM4-4, MGC9247, MGC131945.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSMTLGYWDI RGLAHAIRLL LEYTDSSYEE KKYTMGDAPD YDRSQWLNEK FKLGLDFPNL PYLIDGAHKI TQSNAILCYI ARKHNLCGET EEEKIRVDIL ENQAMDVSNQ LARVCYSPDF EKLKPEYLEE LPTMMQHFSQ FLGKRPWFVG DKITFVDFLA YDVLDLHRIF EPNCLDAFPN LKDFISRFEG LEKISAYMKS SRFLPKPLYT RVAVWGNK.

Product Science Overview

Structure and Expression

GSTM4 is a cytosolic enzyme with a molecular weight of approximately 26 kDa . It is expressed in various tissues and is involved in the detoxification of a wide range of substrates, including carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress . The enzyme is typically expressed in E. coli for recombinant production .

Function and Mechanism

The primary function of GSTM4 is to facilitate the conjugation of GSH to electrophilic compounds, thereby neutralizing their reactivity and making them more water-soluble for excretion . This detoxification process is essential for protecting cells from damage caused by reactive oxygen species (ROS) and other harmful compounds .

Genetic Variability

The genes encoding the mu class of GSTs, including GSTM4, are located on chromosome 1p13.3 and are known to be highly polymorphic . These genetic variations can influence an individual’s susceptibility to carcinogens and toxins, as well as affect the toxicity and efficacy of certain drugs .

Applications

Recombinant human GSTM4 is widely used in research to study its role in detoxification and its potential implications in drug resistance and cancer therapy . It is also utilized in various biochemical assays to investigate the enzyme’s activity and substrate specificity .

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