GSTA1 Human

Glutathione S-Transferase Alpha-1 Human Recombinant
Cat. No.
BT6494
Source
Escherichia Coli.
Synonyms
GST2, GSTA1-1, GTH1, GSTA-1, GSTAI, GSTA-I, EC 2.5.1.18, Glutathione S-transferase A1, GST HA subunit 1, GST-epsilon, GST class-alpha member 1, GSTA1, MGC131939.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 90.0% 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

GSTA1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 222 amino acids (1-222 a.a.) and having a molecular mass of 25.6 kDa. The GSTA1 is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Two separate supergene families encode membrane-bound and cytosolic forms of GST. These enzymes play a crucial role in detoxification by conjugating glutathione with electrophilic compounds, such as carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress. Mammals possess eight distinct classes of soluble cytoplasmic GST: alpha, kappa, mu, omega, pi, sigma, theta, and zeta. GSTA1, clustered on chromosome 6, exhibits high expression levels in the liver and contributes to cellular protection against reactive oxygen species.
Description
Recombinantly produced in E.Coli, GSTA1 Human Recombinant is a single, non-glycosylated polypeptide chain comprising 222 amino acids (1-222 a.a.) with a molecular mass of 25.6 kDa. The purification of GSTA1 is achieved through proprietary chromatographic techniques.
Physical Appearance
A sterile, colorless solution.
Formulation
The GSTA1 solution is provided at a concentration of 1mg/ml and contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, and 10% glycerol.
Stability
For short-term storage (2-4 weeks), the product should be kept at 4°C. For extended storage, it is recommended to freeze the product at -20°C. To ensure optimal stability during long-term storage, adding a carrier protein (0.1% HSA or BSA) is advisable. Multiple freeze-thaw cycles should be avoided.
Purity
SDS-PAGE analysis indicates a purity greater than 90.0%.
Biological Activity

The specific activity, determined by measuring the conjugation of 1.0 µmole of 1-chloro-2,4-dinitrobenzene (CDNB) with reduced glutathione per minute at pH 6.5 and 25°C, is 35,000 pmol/min/µg.

Synonyms
GST2, GSTA1-1, GTH1, GSTA-1, GSTAI, GSTA-I, EC 2.5.1.18, Glutathione S-transferase A1, GST HA subunit 1, GST-epsilon, GST class-alpha member 1, GSTA1, MGC131939.
Source
Escherichia Coli.
Amino Acid Sequence
MAEKPKLHYF NARGRMESTR WLLAAAGVEF EEKFIKSAED LDKLRNDGYL MFQQVPMVEI DGMKLVQTRA ILNYIASKYN LYGKDIKERA LIDMYIEGIA DLGEMILLLP VCPPEEKDAK LALIKEKIKN RYFPAFEKVL KSHGQDYLVG NKLSRADIHL VELLYYVEEL DSSLISSFPL LKALKTRISN LPTVKKFLQP GSPRKPPMDE KSLEEARKIF RF.

Product Science Overview

Introduction

Glutathione S-Transferase Alpha-1 (GSTA1) is a member of the glutathione S-transferase (GST) family of enzymes. These enzymes play a crucial role in the detoxification of a wide range of endogenous and exogenous compounds by catalyzing the conjugation of the tripeptide glutathione (GSH) to electrophilic centers on these compounds .

Gene and Protein Structure

The GSTA1 gene is located on chromosome 6 in humans and is part of a cluster of similar genes and pseudogenes . The gene encodes a protein that is predominantly expressed in the liver and kidney, where it is involved in the detoxification processes . The protein structure of GSTA1 includes a conserved glutathione-binding site and a hydrophobic substrate-binding site, which are essential for its catalytic activity .

Function and Mechanism

GSTA1 catalyzes the nucleophilic attack of the sulfur atom of glutathione on the electrophilic groups of a wide range of substrates, including carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress . This reaction is a critical step in the detoxification pathway, as it renders these compounds more water-soluble and thus easier to excrete from the body .

In addition to its role in detoxification, GSTA1 also exhibits glutathione peroxidase activity, which helps protect cells from reactive oxygen species and the products of lipid peroxidation . This activity is particularly important in protecting cells from oxidative damage and maintaining cellular homeostasis .

Clinical Significance

Polymorphisms in the GSTA1 gene can influence an individual’s ability to metabolize different drugs and detoxify various environmental toxins . These genetic variations can affect the efficacy and toxicity of certain medications, making GSTA1 an important factor in personalized medicine .

Increases in serum and urinary levels of GSTA1 have been associated with hepatocyte and renal proximal tubular necrosis, respectively . Therefore, GSTA1 can serve as a biomarker for monitoring liver and kidney injury .

Applications in Biotechnology

Recombinant human GSTA1 is widely used in research and biotechnology for studying the detoxification pathways and the effects of various compounds on cellular health . It is also used in the development of assays for detecting and quantifying GST activity in biological samples .

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