GSTO2 Human

Glutathione S-Transferase Omega 2 Human Recombinant
Cat. No.
BT7866
Source
Escherichia Coli.
Synonyms
Glutathione S-transferase omega-2, GSTO-2, Glutathione S-transferase omega 2-2, GSTO 2-2, Glutathione-dependent dehydroascorbate reductase, Monomethylarsonic acid reductase, MMA(V) reductase, GSTO2, bA127L20.1.
Appearance
Sterile Filtered clear solution.
Purity
Greater than 85.0% 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.
Shipped with Ice Packs
In Stock

Description

GSTO2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 266 amino acids (1-243) and having a molecular mass of 30.6kDa.
GSTO2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Glutathione S-transferase omega 2 (GSTO2) is a member of the GST superfamily that plays a crucial role in detoxification and metabolism. It catalyzes the conjugation of glutathione with various organic compounds, forming thioethers. This process is essential for eliminating xenobiotics and carcinogens from the body. GSTO2 exhibits glutathione-dependent thiol transferase activity and possesses high dehydroascorbate reductase activity, suggesting its involvement in ascorbic acid recycling. Moreover, it participates in inorganic arsenic biotransformation and reduces monomethylarsonic acid (MMA). GSTO2 is widely expressed in tissues like the liver, kidney, skeletal muscle, and prostate, with the highest expression observed in the testis.
Description
Recombinant human GSTO2, expressed in E. coli, is a single, non-glycosylated polypeptide chain consisting of 266 amino acids (residues 1-243) with a molecular weight of 30.6 kDa. It includes a 23 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Physical Appearance
Clear, sterile-filtered solution.
Formulation
The GSTO2 solution is provided at a concentration of 0.25 mg/ml in a buffer containing 20 mM Tris-HCl (pH 8.0), 0.1 M NaCl, and 40% glycerol.
Stability
For short-term storage (up to 2-4 weeks), keep at 4°C. For long-term storage, freeze at -20°C. Adding a carrier protein like HSA or BSA (0.1%) is recommended for extended storage. Avoid repeated freeze-thaw cycles.
Purity
Purity is determined to be greater than 85.0% by SDS-PAGE analysis.
Synonyms
Glutathione S-transferase omega-2, GSTO-2, Glutathione S-transferase omega 2-2, GSTO 2-2, Glutathione-dependent dehydroascorbate reductase, Monomethylarsonic acid reductase, MMA(V) reductase, GSTO2, bA127L20.1.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSGDATR TLGKGSQPPG PVPEGLIRIY SMRFCPYSHR TRLVLKAKDI RHEVVNINLR NKPEWYYTKH PFGHIPVLET SQCQLIYESV IACEYLDDAY PGRKLFPYDP YERARQKMLL ELFCKVPHLT KECLVALRCG RECTNLKAAL RQEFSNLEEI
LEYQNTTFFG GTCISMIDYL LWPWFERLDV YGILDCVSHT PALRLWISAM KWDPTVCALL MDKSIFQGFL NLYFQNNPNA FDFGLC.

Product Science Overview

Introduction

Glutathione S-Transferase Omega 2 (GSTO2) is an enzyme belonging to the omega class of the Glutathione S-Transferase (GST) family. GSTs are a diverse group of enzymes that play a crucial role in detoxification processes by catalyzing the conjugation of glutathione (GSH) to various endogenous and exogenous compounds. This conjugation helps in the detoxification of harmful substances, making them more water-soluble and easier to excrete from the body .

Structure and Function

GSTO2 is encoded by the GSTO2 gene located on human chromosome 10q24.3 . The enzyme is characterized by its ability to catalyze the reduction of monomethylarsonic acid (MMA) to dimethylarsinic acid (DMA), a process important for arsenic biotransformation and detoxification . GSTO2 also exhibits dehydroascorbate reductase activity, which is involved in the regeneration of ascorbic acid (vitamin C), an essential antioxidant in the human body .

Biochemical Properties

The recombinant form of GSTO2 is typically expressed in Escherichia coli (E. coli) and purified for research and therapeutic applications . The enzyme’s activity can be measured using various biochemical assays, such as the Glutathione-S-Transferase Assay Kit . GSTO2 has been shown to have a high affinity for substrates like glutathione and various electrophilic compounds, making it a versatile enzyme in detoxification pathways .

Clinical Significance

GSTO2 has been implicated in several physiological and pathological processes. Its role in arsenic detoxification is particularly significant, as arsenic exposure is a major public health concern in many parts of the world . Additionally, variations in the GSTO2 gene have been associated with susceptibility to various diseases, including cancer and neurodegenerative disorders . Understanding the function and regulation of GSTO2 can provide insights into the mechanisms of these diseases and potential therapeutic targets .

Applications in Biotechnology

Recombinant GSTO2 is widely used in research to study its enzymatic properties and potential therapeutic applications. It is also utilized in the development of biosensors for detecting environmental toxins and in the production of transgenic plants with enhanced detoxification capabilities . The enzyme’s ability to regenerate ascorbic acid makes it a valuable tool in antioxidant research and applications .

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