GSTA4 Human, Active

Glutathione S-Transferase Alpha 4 Human Recombinant, Active
Cat. No.
BT6764
Source
Escherichia Coli.
Synonyms
Glutathione S-transferase A4, GST class-alpha member 4, Glutathione S-transferase A4-4, GSTA4, GSTA4-4.
Appearance
Sterile Filtered clear solution.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Usage
Prospec'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.
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Description

GSTA4 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 246 amino acids (1-222) and having a molecular mass of 28.3kDa.
GSTA4 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Glutathione S-transferase A4 (GSTA4) is a member of the GST enzyme family. These enzymes play a crucial role in cellular detoxification by acting upon a variety of potentially harmful compounds, including those that are toxic, carcinogenic, or pharmacologically active. GSTA4 exhibits particularly high activity towards reactive carbonyl compounds, such as alk-2-enals. Notably, it demonstrates remarkable efficiency in catalyzing the conjugation of reduced glutathione to 4-hydroxynonenal, a significant product of arachidonic acid peroxidation and a widely recognized biomarker for oxidative stress in tissues. GSTA4 expression is most prominent in the brain, placenta, and skeletal muscle, with considerably lower levels observed in the lung and liver.
Description
Recombinant human GSTA4, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 222 amino acids (representing the core protein sequence, excluding any tags), with an additional 24 amino acid His-tag fused at the N-terminus, resulting in a total molecular weight of 28.3kDa. The purification process involves proprietary chromatographic techniques to ensure high purity.
Physical Appearance
A clear solution that has been sterilized by filtration.
Formulation
The GSTA4 solution is provided at a concentration of 1mg/ml and is formulated in a buffer containing 20mM Tris-HCl (pH 8.0), 20% glycerol, 2mM DTT, and 100mM NaCl.
Stability
For short-term storage (up to 2-4 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 advised for long-term storage. To maintain product integrity, avoid repeated cycles of freezing and thawing.
Purity
Purity is determined by SDS-PAGE analysis and is guaranteed to be greater than 95%.
Biological Activity
The specific activity of the enzyme is determined to be greater than 4,000 pmol/min/ug. This is measured as the enzyme's capacity to conjugate 1.0 micromole 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 A4, GST class-alpha member 4, Glutathione S-transferase A4-4, GSTA4, GSTA4-4.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMAARPK LHYPNGRGRM ESVRWVLAAA GVEFDEEFLE TKEQLYKLQD GNHLLFQQVP MVEIDGMKLV QTRSILHYIA DKHNLFGKNL KERTLIDMYV EGTLDLLELL IMHPFLKPDD QQKEVVNMAQ KAIIRYFPVF EKILRGHGQS FLVGNQLSLA DVILLQTILA LEEKIPNILS AFPFLQEYTV KLSNIPTIKR FLEPGSKKKP PPDEIYVRTV YNIFRP.

Product Science Overview

Introduction

Glutathione S-Transferase Alpha 4 (GSTA4) is an enzyme encoded by the GSTA4 gene in humans . This enzyme belongs to the family of Glutathione S-Transferases (GSTs), which play a crucial role in the detoxification processes within the body . The recombinant form of this enzyme, which is produced through genetic engineering techniques, is often used in research and industrial applications due to its high activity and stability.

Structure and Function

GSTA4 is a cytosolic enzyme that catalyzes the conjugation of reduced glutathione (GSH) to a wide variety of hydrophobic and electrophilic compounds . This conjugation process is essential for making these compounds more water-soluble, thereby facilitating their excretion from the body . The enzyme has a high catalytic efficiency with 4-hydroxyalkenals, such as 4-hydroxynonenal (4-HNE), which are products of lipid peroxidation .

Genetic and Molecular Characteristics

The GSTA4 gene is located on chromosome 6 and is part of a cluster of alpha class genes . These genes encode enzymes with glutathione peroxidase activity, which are involved in the detoxification of lipid peroxidation products . The alpha class of GSTs, including GSTA4, is highly related and shares significant sequence homology .

Biological Significance

GSTA4 plays a vital role in cellular defense mechanisms against toxic, carcinogenic, and pharmacologically active electrophilic compounds . The enzyme’s activity is particularly important in protecting cells from oxidative stress and damage caused by reactive electrophiles . This protection is crucial in preventing degenerative diseases such as Parkinson’s disease, Alzheimer’s disease, cataract formation, and atherosclerosis .

Recombinant Production

The recombinant form of GSTA4 is produced using genetic engineering techniques that involve inserting the GSTA4 gene into a suitable expression system, such as bacteria or yeast . This allows for the large-scale production of the enzyme with high purity and activity. Recombinant GSTA4 is widely used in research to study its biochemical properties and potential therapeutic applications .

Applications

Recombinant GSTA4 is used in various applications, including:

  • Biochemical Research: Studying the enzyme’s structure, function, and interaction with other molecules.
  • Drug Development: Screening for potential inhibitors or activators of GSTA4 that could be used in therapeutic interventions.
  • Toxicology: Assessing the detoxification capacity of GSTA4 in response to various toxic compounds.

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GSTA4 Human
Glutathione S-Transferase Alpha 4 Human Recombinant
Cat. No.
BT6669
Source
Escherichia Coli.
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