GSTP1 Human

Glutathione S-Transferase pi 1 Human Recombinant
Cat. No.
BT7949
Source
Escherichia Coli.
Synonyms
Glutathione S-transferase P, GST class-pi, GSTP1-1, GSTP1, FAEES3, GST3, PI, DFN7.
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.
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Description

GSTP1 Human Recombinant fused with 36 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 246 amino acids

(1-210 a.a.) And having a molecular mass of 27.4kDa.

The GSTP1 is purified by proprietary chromatographic techniques.

Product Specs

Introduction
GSTP1, a polymorphic gene, encodes active GSTP1 variant proteins with functional differences. These proteins are believed to play a role in xenobiotic metabolism and may contribute to susceptibility to cancer and other diseases. GSTP1 belongs to the pi class of glutathione S-transferases (GSTs). GST enzymes are important for detoxification as they catalyze the conjugation of various hydrophobic and electrophilic compounds with reduced glutathione. Based on their biochemical, immunologic, and structural properties, soluble GSTs are classified into four main classes: alpha, mu, pi, and theta. GSTP1 catalyzes the reaction between glutathione and an acceptor molecule, resulting in the formation of Sulfur-substituted glutathione. Reactions involving glutathione contribute to the transformation of a wide range of electrophiles, such as reactive products of lipids, proteins, carcinogens, therapeutic drugs, environmental toxins, and oxidative stress products. Inactivation of GSTP1 due to CpG hypermethylation is common in pituitary adenomas and may contribute to aggressive tumor behavior. GSTP1 is potentially a transcriptional target of the tumor suppressor gene p53. Single-nucleotide polymorphisms in GSTP1 are associated with altered protein binding, affecting GSTP1's role in carcinogen and drug metabolism. This may have implications for disease pathogenesis and/or drug response. GST-pi may play a central role in the proliferation of androgen-independent prostate cancer cells.
Description
GSTP1 Human Recombinant protein is produced in E. coli and fused with a 36 amino acid His tag at its N-terminus. This results in a single, non-glycosylated polypeptide chain containing 246 amino acids (1-210 a.a.) with a molecular mass of 27.4 kDa. The protein is purified using proprietary chromatographic techniques.
Physical Appearance
Clear, colorless solution, sterile-filtered.
Formulation
The GSTP1 solution is provided at a concentration of 0.5 mg/ml and contains 20 mM Tris-HCl buffer (pH 7.0), 30% glycerol, 1 mM EDTA, and 0.1 mM PMSF.
Stability
For short-term storage (2-4 weeks), the GSTP1 solution should be stored at 4°C. For long-term storage, it is recommended to store the protein 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 GSTP1 is greater than 95% as determined by SDS-PAGE analysis.
Biological Activity
The specific activity of GSTP1 is greater than 80 units/mg. One unit of activity is defined as the amount of enzyme required to conjugate 1.0 µmole of 1-chloro-2,4-dinitrobenzene (CDNB) with reduced glutathione per minute at pH 6.5 and 25°C.
Synonyms
Glutathione S-transferase P, GST class-pi, GSTP1-1, GSTP1, FAEES3, GST3, PI, DFN7.
Source
Escherichia Coli.
Amino Acid Sequence

MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMPPY TVVYFPVRGR CAALRMLLAD QGQSWKEEVV TVETWQEGSL KASCLYGQLP KFQDGDLTLY QSNTILRHLG RTLGLYGKDQ QEAALVDMVN DGVEDLRCKY ISLIYTNYEA GKDDYVKALP GQLKPFETLL SQNQGGKTFI VGDQISFADY NLLDLLLIHE VLAPGCLDAF PLLSAYVGRL SARPKLKAFL ASPEYVNLPI NGNGKQ.

Product Science Overview

Introduction

Glutathione S-Transferase pi 1 (GSTP1) is a member of the glutathione S-transferase (GST) family, which plays a crucial role in the detoxification process by catalyzing the conjugation of reduced glutathione to various electrophilic compounds. This enzyme is encoded by the GSTP1 gene in humans and is involved in the metabolism of xenobiotics and protection against oxidative stress.

Gene and Protein Structure

The GSTP1 gene is located on chromosome 11q13 and is known to be polymorphic, encoding functionally different variant proteins . These variants are thought to influence an individual’s susceptibility to various diseases, including cancer . The GSTP1 protein is a cytosolic enzyme that belongs to the pi class of GSTs, which also includes alpha, mu, and theta classes .

Function and Mechanism

GSTP1 plays a significant role in the detoxification of endogenous and exogenous compounds. It catalyzes the conjugation of glutathione to a wide range of substrates, including environmental toxins, carcinogens, and products of oxidative stress . This process helps in the neutralization and elimination of harmful compounds from the body.

Clinical Significance

The polymorphic nature of the GSTP1 gene has been associated with varying levels of enzyme activity and, consequently, different susceptibilities to diseases. For instance, certain GSTP1 variants have been linked to an increased risk of developing cancers, such as lung, breast, and prostate cancer . Additionally, GSTP1 is being studied as a potential drug target for cancer therapy, particularly in triple-negative breast cancer .

Recombinant GSTP1

Recombinant GSTP1 is produced using recombinant DNA technology, which involves inserting the GSTP1 gene into an expression vector and introducing it into a host cell, such as E. coli, for protein production. This recombinant protein is used in various research applications, including studies on enzyme kinetics, drug metabolism, and the development of GSTP1 inhibitors for therapeutic purposes .

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