GST

Glutathione S-Transferase Recombinant
Cat. No.
BT5474
Source
Escherichia Coli.
Synonyms

Glutathione S-Transferase, GST, Glutathione S-transferase class-mu 26 kDa isozyme, GST 26, Sj26 antigen, SjGST.

Appearance
Sterile Filtered clear solution.
Purity
Greater than 95% 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.
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Description

Recombinant Glutathione S-Transferase full length protein (1-218a.a.) expressed in E.coli, having a molecular mass of 26kDa. GST was isolated from an E. coli strain that carries the coding sequence for Schistosoma japonicum GST under the control of a T7 promoter.
The GST is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Glutathione S-Transferase (GST) is an antioxidant enzyme believed to play a crucial role in cellular defense against reactive oxygen species. It exhibits Se-independent glutathione peroxidase activity, reducing lipid hydroperoxides. GST also detoxifies byproducts of lipid peroxidation, such as 4-hydroxynonenal (4-HNE). This soluble enzyme, with a molecular weight of 26 kDa, exists as a dimer in aerobic organisms. Each monomer comprises two domains: one binds GSH and structurally resembles thioredoxin (α/β structure), while the other, entirely helical, binds hydrophobic substrates. The GST-fusion protein expression system is widely employed for recombinant protein expression. It facilitates the expression of peptides or regulatory protein domains fused to the C-terminus of Schistosoma japonicum GST. These fusion proteins retain GST's enzymatic activity and dimerization ability, mirroring in vivo behavior. Purification is achieved through GST-affinity column chromatography. In many cases, specific proteases are used to cleave the linker between the protein domain and GST, separating the desired peptides or domains. This technique has broad applications in generating various proteins for crystallization, molecular immunology research, vaccine production, and studies investigating protein-protein and protein-DNA interactions.
Description
This product consists of recombinant, full-length Glutathione S-Transferase (amino acids 1-218) with a molecular weight of 26 kDa. It is expressed in E. coli from a strain containing the coding sequence for Schistosoma japonicum GST under the control of a T7 promoter. Purification is carried out using proprietary chromatographic techniques.
Physical Appearance
A clear solution that has undergone sterile filtration.
Formulation
The GST protein is supplied in Phosphate Buffered Saline with a pH of 7.4.
Stability
For optimal storage, keep the product refrigerated at 4°C if the entire vial will be used within 2-4 weeks. For longer storage periods, freezing at -20°C is recommended. Consider adding a carrier protein (0.1% HSA or BSA) for extended storage. It's crucial to avoid repeated freeze-thaw cycles to maintain product integrity.
Purity
The purity of this product is determined to be greater than 95% through SDS-PAGE analysis.
Biological Activity
The specific activity of this enzyme is greater than 20 units per milligram. One unit is defined as the amount of enzyme required to conjugate 1.0 micromole of 1-chloro-2,4-dinitrobenzene (CDNB) with reduced glutathione per minute at a pH of 6.5 and a temperature of 25°C.
Synonyms

Glutathione S-Transferase, GST, Glutathione S-transferase class-mu 26 kDa isozyme, GST 26, Sj26 antigen, SjGST.

Source
Escherichia Coli.
Amino Acid Sequence

MSPILGYWKI KGLVQPTRLL LEYLEEKYEE HLYERDEGDK WRNKKFELGL EFPNLPYYID GDVKLTQSMA IIRYIADKHN MLGGCPKERA EISMLEGAVL DIRYGVSRIA YSKDFETLKV DFLSKLPEML KMFEDRLCHK TYLNGDHVTH PDFMLYDALD VVLYMDPMCL DAFPKLVCFK KRIEAIPQID KYLKSSKYIA WPLQGWQATF GGGDHPPKSD LVPR.

Product Science Overview

Introduction

Glutathione S-Transferases (GSTs) are a superfamily of enzymes that play a crucial role in detoxification processes by catalyzing the conjugation of glutathione to various electrophilic compounds. These compounds include metabolites generated by oxidative processes, environmental toxins, carcinogens, and anti-cancer drugs . GSTs are found in both eukaryotes and prokaryotes and are involved in a wide range of biological functions, including protection against biotic and abiotic stresses, secondary metabolite transportation, and regulation of redox homeostasis .

Evolution and Structure

GSTs are considered one of the most ancient protein superfamilies, having evolved principally from gene duplication of an ancestral glutathione (GSH) binding protein . They have a highly conserved integrated architecture with separate binding pockets for substrates and ligands. The structural fidelity of GSTs is maintained with high thermal stability (Tm values ranging from 50º to 60º), making them versatile proteins for various biotechnological applications .

Functional Roles

GSTs are multifunctional enzymes with diverse roles in cellular metabolism. They are involved in:

  • Detoxification: Conjugating glutathione to toxic compounds, making them more water-soluble and easier to excrete .
  • Stress Response: Protecting cells against oxidative stress and other environmental stresses .
  • Secondary Metabolism: Participating in the biosynthesis and transport of secondary metabolites such as anthocyanins .
  • Cell Signaling: Regulating cell signaling pathways and maintaining redox homeostasis .
Recombinant GSTs

Recombinant GSTs are produced using genetic engineering techniques to express GST proteins in various host systems, such as bacteria, yeast, or mammalian cells. These recombinant proteins are used in research and industrial applications, including:

  • Protein Purification: GST tags are commonly used in affinity chromatography to purify recombinant proteins .
  • Drug Development: Studying the interaction of GSTs with potential drug candidates to develop new therapeutic agents .
  • Biotechnological Applications: Utilizing GSTs in bioremediation, agriculture, and nanotechnology .

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