GSTT1 Human

Glutathione S-Transferase Theta-1 Human Recombinant
Cat. No.
BT8225
Source
Escherichia Coli.
Synonyms
Glutathione S-transferase theta-1, GST class-theta-1, Glutathione transferase T1-1, GSTT1.
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

GSTT1 Human Recombinant fused with 37 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 277 amino acids (1-240 a.a.) and having a molecular mass of 31.5kDa.
The GSTT1 is purified by proprietary chromatographic techniques.

Product Specs

Introduction
GSTT1, a member of a protein superfamily, facilitates the conjugation of reduced glutathione to various electrophilic and hydrophobic compounds. Classified as one of the four main GST classes (alpha, mu, pi, and theta), GSTT1 plays a crucial role in detoxification and activation reactions. It catalyzes the conjugation of glutathione with industrial chemicals such as epoxybutane, ethylene oxides, and halomethane. This enzyme is primarily found in erythrocytes, with lower levels detected in the liver and Clara cells at the alveolar/bronchiolar junction in the lung. Notably, approximately 38% of the population exhibits a deficiency in the GSTT1 gene. This deficiency has been linked to an increased risk of developing acquired aplastic anemia and acute myeloid leukemia. Individuals can be categorized into GSTT1+ (conjugator) and GSTT1- (non-conjugator) phenotypes based on the presence or absence of the GSTT1 gene. The GSTT1+ phenotype is characterized by its ability to catalyze the glutathione conjugation of dichloromethane. Conversely, individuals with GSTT1-null genotypes are considered to have a higher susceptibility to leukoplakia. Furthermore, studies have identified a connection between germline genetic polymorphism in GSTT1 and an elevated risk of breast cancer.
Description
Recombinant human GSTT1, expressed in E. coli and fused with a 37 amino acid His tag at the N-terminus, is available as a non-glycosylated polypeptide chain. This single-chain protein comprises 277 amino acids (1-240 a.a.) and exhibits a molecular weight of 31.5kDa. Purification of GSTT1 is achieved through proprietary chromatographic techniques.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
The GSTT1 solution is supplied in a buffer consisting of 20mM Tris-HCl (pH 8.0) and 10% glycerol.
Stability
For short-term storage (2-4 weeks), the GSTT1 vial can be stored at 4°C. For extended storage, freezing at -20°C is recommended. To further enhance stability during long-term storage, the addition of a carrier protein like HSA or BSA (0.1%) is advisable. It is important to minimize repeated freeze-thaw cycles to preserve protein integrity.
Purity
The purity of GSTT1 exceeds 95.0%, as determined by SDS-PAGE analysis.
Synonyms
Glutathione S-transferase theta-1, GST class-theta-1, Glutathione transferase T1-1, GSTT1.
Source
Escherichia Coli.
Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMGL ELYLDLLSQP CRAVYIFAKK NDIPFELRIV DLIKGQHLSD ACAQVNPLKK VPALKDGDFT LTESVAILLY LTRKYKVPDY WYPQDLQARA RVDEYLAWQH TTLRRSCLRA LWHKVMFPVF LGEPVSPQTL AATLAELDVT LQLLEDKFLQ NKAFLTGPHI SLADLVAITE LMHPVGAGCQ VFEGRPKLAT WRQRVEAAVG EDLFQEAHEV ILKAKDFPPA DPTIKQKLMP WVLAMIR.

Product Science Overview

Introduction

Glutathione S-Transferase Theta-1 (GSTT1) is an enzyme encoded by the GSTT1 gene in humans. This enzyme belongs to the glutathione S-transferase (GST) family, which plays a crucial role in the detoxification process by catalyzing the conjugation of reduced glutathione to a variety of hydrophobic and electrophilic compounds .

Gene and Protein Structure

The GSTT1 gene is located on chromosome 22q11.23 and spans approximately 8092 base pairs. It contains five exons and four introns . The gene encodes a protein consisting of 240 amino acids with a molecular weight of approximately 25 kDa . The GSTT1 protein is primarily expressed in the liver .

Function and Mechanism

GSTT1 is involved in the detoxification of endogenous and exogenous compounds. It catalyzes the conjugation of reduced glutathione (GSH) to various substrates, facilitating their solubility and excretion from the body . This process is essential for the metabolism of xenobiotics and protection against oxidative stress .

Recombinant GSTT1

Recombinant human GSTT1 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 recombinant form retains the enzymatic activity of the native protein, making it valuable for research and industrial applications .

Clinical Significance

Mutations or deletions in the GSTT1 gene have been associated with an increased risk of certain cancers, including lung, head, and neck cancers . The enzyme’s role in detoxification and xenobiotic metabolism suggests that variations in GSTT1 activity may influence individual susceptibility to environmental toxins and carcinogens .

Applications

Recombinant GSTT1 is widely used in research to study the enzyme’s structure, function, and role in disease. It is also employed in drug development and toxicology studies to evaluate the metabolism and detoxification of new compounds .

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