GSTP1 Mouse

Glutathione S-Transferase pi 1 Mouse Recombinant
Cat. No.
BT8038
Source
Escherichia Coli.
Synonyms
Glutathione S-transferase P 1, Gst P1, GST YF-YF, GST class-pi, GST-piB, Preadipocyte growth factor.
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.
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Description

GSTP1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 233 amino acids (1-210 a.a) and having a molecular mass of 26kDa.
GSTP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
The GSTP1 gene exhibits polymorphism, resulting in variant GSTP1 proteins with differing activities and functions. These proteins are thought to play a role in the metabolism of xenobiotics, potentially influencing susceptibility to cancer and other diseases. GSTP1 belongs to the pi class of glutathione S-transferases (GSTs). GST enzymes are crucial for detoxification processes, catalyzing the conjugation of various hydrophobic and electrophilic compounds with reduced glutathione. Soluble GSTs are classified into four main classes based on their biochemical, immunological, and structural characteristics: alpha, mu, pi, and theta. GSTP1 facilitates the conjugation of glutathione with acceptor molecules, forming Sulfur-substituted glutathione. These glutathione-dependent reactions contribute to the transformation of a wide array of electrophiles, including reactive byproducts of lipids, proteins, carcinogens, therapeutic drugs, environmental toxins, and oxidative stress. Notably, GSTP1 inactivation due to CpG hypermethylation is prevalent in pituitary adenomas and might contribute to aggressive tumor behavior. Furthermore, GSTP1 may be transcriptionally regulated by the p53 tumor suppressor gene. Single-nucleotide polymorphisms (SNPs) in GSTP1 can alter protein binding, thereby affecting its role in carcinogen and drug metabolism. Consequently, these SNPs may have implications for disease pathogenesis and drug response. GST-pi could be centrally involved in the proliferation of androgen-independent prostate cancer cells.
Description
Recombinant Mouse GSTP1, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 233 amino acids, comprising amino acids 1 to 210, and has a molecular weight of 26 kDa. This GSTP1 protein is fused to a 23 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Physical Appearance
A clear, sterile-filtered solution.
Formulation
The GSTP1 protein solution has a concentration of 1 mg/ml and is prepared in Phosphate Buffered Saline (pH 7.4) with 10% glycerol.
Stability
For short-term storage (up to 2-4 weeks), the entire vial can be stored at 4°C. For longer storage, it is recommended to freeze the solution at -20°C. To ensure stability during long-term storage, the addition of a carrier protein (0.1% HSA or BSA) is advisable. It is essential to avoid repeated freeze-thaw cycles.
Purity
The purity of the protein is determined by SDS-PAGE analysis and is greater than 90.0%.
Biological Activity
The specific activity, a measure of enzyme 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 a pH of 6.5 and a temperature of 25°C. The specific activity of this product is greater than 40 units/mg.
Synonyms
Glutathione S-transferase P 1, Gst P1, GST YF-YF, GST class-pi, GST-piB, Preadipocyte growth factor.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMPPYTIV YFPVRGRCEA MRMLLADQGQ SWKEEVVTID TWMQGLLKPT CLYGQLPKFE DGDLTLYQSN AILRHLGRSL GLYGKNQREA AQMDMVNDGV EDLRGKYVTL IYTNYENGKN DYVKALPGHL KPFETLLSQN QGGKAFIVGD QISFADYNLL DLLLIHQVLA PGCLDNFPLL SAYVARLSAR PKIKAFLSSP EHVNRPINGN GKQ.

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 of endogenous and exogenous compounds. GSTs are phase II detoxification enzymes that catalyze the conjugation of glutathione (GSH) to various electrophilic compounds, facilitating their excretion from the body .

Structure and Function

GSTP1 is one of the most abundant members of the cytosolic GSTs in mammalian cells. It has a GSH-binding site and a substrate-binding site (H-site) that catalyze the nucleophilic attack of the sulfur atom of GSH on electrophilic groups of substrate molecules . The enzyme’s activity is essential for the metabolism of drugs, xenobiotics, and carcinogens, making it a critical component in cellular defense mechanisms .

Role in Disease and Toxicology

GSTP1 has been implicated in various diseases, including cancer and liver toxicity. In mouse models, the expression of GSTP1 varies significantly between species, with high expression in mouse liver hepatocytes and low or no expression in human liver hepatocytes . This difference in expression patterns has been shown to influence the liver’s response to drugs and toxins. For instance, mice with disrupted Gstp genes exhibit altered liver toxicity in response to acetaminophen overdose, highlighting the enzyme’s role in hepatocyte injury .

Anti-inflammatory Properties

Recent studies have demonstrated that GSTP1 also possesses anti-inflammatory properties. It has been shown to play a protective role in inflammation by preventing the release of high mobility group box-1 protein (HMGB1), a key cytokine involved in septic death . GSTP1 achieves this by binding to HMGB1 in the nucleus and suppressing its phosphorylation, thereby preventing its translocation to the cytoplasm and subsequent release .

Recombinant GSTP1

Recombinant GSTP1, particularly from mouse sources, is widely used in research to study its biochemical properties and therapeutic potential. The recombinant form allows for the production of large quantities of the enzyme, facilitating detailed studies on its structure, function, and role in various biological processes.

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