GPX3 Human

Glutathione Peroxidase 3 Human Recombinant
Cat. No.
BT18592
Source
Escherichia Coli.
Synonyms
Glutathione peroxidase 3, GPx-3, GSHPx-3, Extracellular glutathione peroxidase, Plasma glutathione peroxidase, GPx-P, GSHPx-P, GPX3, GPXP.
Appearance
Sterile filtered colorless solution.
Purity
Greater than 85% 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.
Shipped with Ice Packs
In Stock

Description

GPX3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 227 amino acids (21-226) and having a molecular mass of 25.7kDa.
GPX3 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Glutathione peroxidase 3 (GPX3), a member of the glutathione peroxidase family, plays a crucial role in detoxifying hydrogen peroxide. It protects cells and enzymes from oxidative damage by catalyzing the reduction of hydrogen peroxide, lipid peroxides, and organic hydroperoxide using glutathione. GPX3 is notable for containing selenocysteine at its active site, a rare occurrence in higher vertebrates. This selenocysteine is encoded by the stop codon TGA.
Description
Recombinant human GPX3, produced in E. coli, is a single, non-glycosylated polypeptide chain. It comprises 227 amino acids (21-226), resulting in a molecular weight of 25.7 kDa. The protein includes a 21 amino acid His-tag at the N-terminus and undergoes purification using proprietary chromatographic techniques.
Physical Appearance
Clear, colorless solution that has been sterilized by filtration.
Formulation
The GPX3 solution is supplied in a buffer containing 20mM Tris-HCl (pH 7.5), 40% glycerol, 0.15M NaCl, and 1mM DTT.
Stability
For short-term storage (2-4 weeks), the product can be kept 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. Repeated freezing and thawing should be avoided.
Purity
The purity of the product is greater than 85% as determined by SDS-PAGE analysis.
Synonyms
Glutathione peroxidase 3, GPx-3, GSHPx-3, Extracellular glutathione peroxidase, Plasma glutathione peroxidase, GPx-P, GSHPx-P, GPX3, GPXP.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MQSRGQEKSK MDCHGGISGT IYEYGALTID GEEYIPFKQY AGKYVLFVNV ASYCGLTGQY IELNALQEEL APFGLVILGF PCNQFGKQEP GENSEILPTL KYVRPGGGFV PNFQLFEKGD VNGEKEQKFY TFLKNSCPPT SELLGTSDRL FWEPMKVHDI RWNFEKFLVG PDGIPIMRWH HRTTVSNVKM DILSYMRRQA ALGVKRK.

Product Science Overview

Introduction

Glutathione Peroxidase 3 (GPX3), also known as plasma glutathione peroxidase (GPx-P) or extracellular glutathione peroxidase, is an enzyme encoded by the GPX3 gene in humans . It belongs to the glutathione peroxidase family, which plays a crucial role in protecting cells from oxidative damage by reducing hydrogen peroxide, lipid peroxides, and organic hydroperoxides .

Structure and Function

GPX3 contains a selenocysteine (Sec) residue at its active site, which is essential for its enzymatic activity . The selenocysteine is encoded by the UGA codon, which typically signals translation termination. However, in the case of Sec-containing genes, a specific stem-loop structure in the 3’ untranslated region (UTR), known as the Sec insertion sequence (SECIS), allows the UGA codon to be recognized as a Sec codon instead of a stop signal .

GPX3 functions as an oxidoreductase enzyme, catalyzing the conversion of hydrogen peroxide into water, thereby mitigating oxidative damage . It has a wide thiol specificity, with sources of reducing power including glutathione (GSH), cysteine, mercaptoethanol, and dithiothreitol . In vitro studies have shown that GSH can be completely replaced by reduced homocysteine for GPX3 activity .

Biological Significance

GPX3 is primarily found in the extracellular space, including blood plasma, and is involved in detoxifying hydrogen peroxide in the extracellular environment . It plays a vital role in maintaining the redox balance and protecting cells from oxidative stress . Beyond its antioxidant function, GPX3 is also involved in regulating metabolism, modulating cell growth, inducing apoptosis, and facilitating signal transduction .

Clinical Relevance

Recent studies have highlighted the significance of GPX3 in various non-neoplastic diseases. Aberrant expression of GPX3 has been associated with multiple pathological processes, including cardiovascular diseases, metabolic disorders, and inflammatory conditions . Additionally, GPX3 serves as a significant tumor suppressor in various cancers, making it a potential diagnostic biomarker and therapeutic target .

Recombinant GPX3

Recombinant human GPX3 is produced using recombinant DNA technology, allowing for the large-scale production of this enzyme for research and therapeutic purposes . Recombinant GPX3 retains the same structure and function as the naturally occurring enzyme, making it a valuable tool for studying oxidative stress and developing potential treatments for diseases associated with oxidative damage .

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