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G6511

Sigma-Aldrich

Glutathione S-Transferase from equine liver

lyophilized powder, ≥25 units/mg protein

Synonym(s):

GST, Glutathione R-transferase, Glutathione S-alkenetransferase, Glutathione S-alkyltransferase, Glutathione S-aralkyltransferase, Glutathione S-aryltransferase, Glutathione S-epoxidetransferase

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About This Item

CAS Number:
Enzyme Commission number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.47

biological source

equine liver

Quality Level

form

lyophilized powder

specific activity

≥25 units/mg protein

mol wt

45-50 kDa

composition

Protein, ≥60%

storage temp.

−20°C

General description

Glutathione S-transferase (GST) is a major detoxification enzyme, and exists as multiple cytoplasmic and membrane-bound isozymes. These isozymes differ in their catalytic activity, as well as in their non-catalytic binding properties. Cytoplasmic isoforms of GST are encoded by five genes, namely α, θ, μ, σ and π. α, μ and π are the most abundant forms in mammals. Membrane bound GST forms are encoded by a single gene.

Biochem/physiol Actions

Glutathione S-transferase (GST) from equine liver has been used-
  • as a constituent of Tris buffer for incubation of human umbilical vein endothelial cells (HUVEC) with atracurium to assess the proliferation of HUVEC in the presence of atracurium
  • as a component of GSB stock solution to determine GSB (glutathione S-bimane) conjugate fluorescence intensity in intact Arabidopsis cells
  • as an enzyme standard in spectrophotometric assay to determine the activity of GST
Glutathione S-transferases are a family of proteins that catalyze the conjugation of reduced glutathione with a variety of hydrophobic chemicals containing electrophilic centers.

Unit Definition

One unit will conjugate 1.0 μmole of 1-chloro-2,4-dinitrobenzene with reduced glutathione per min at pH 6.5 at 25°C.

Physical form

Lyophilized powder containing Tris, reduced glutathione and EDTA.

Analysis Note

Protein determined by biuret.
Purified and assayed by a modification of the method of Simons and Vander Jagt.
Enzymatic activities are based on the conjugation of reduced glutathione with a second substrate. The individual proteins generally have activity with more than one class of substrate.

inhibitor

related product

Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Precautionary Statements

Hazard Classifications

Resp. Sens. 1

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Information

动植物源性产品

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Molecular cloning and characterization of a Glutathione S-transferase gene from Hessian fly (Diptera: Cecidomyiidae)
Yoshiyama M and Shukle R H
Annals of the Entomological Society of America, 97(6), 1285-1293 (2004)
A Amann et al.
Anesthesia and analgesia, 93(3), 690-696 (2001-08-29)
We tested the influence of atracurium and cisatracurium (final concentrations: 0, 0.96, 3.2, 9.6, 32, and 96 microM) on proliferation of human cells (hepatoma HepG2 cells and human umbilical vein endothelial cells) in vitro. In additional experiments, glutathione, N-acetylcysteine, or
Carlota Roca et al.
Pharmaceutics, 14(11) (2022-11-27)
The methyl erythritol phosphate (MEP) pathway of isoprenoid biosynthesis is essential for malaria parasites and also for several human pathogenic bacteria, thus representing an interesting target for future antimalarials and antibiotics and for diagnostic strategies. We have developed a DNA
J D Hayes et al.
Critical reviews in biochemistry and molecular biology, 30(6), 445-600 (1995-01-01)
The glutathione S-transferases (GST) represent a major group of detoxification enzymes. All eukaryotic species possess multiple cytosolic and membrane-bound GST isoenzymes, each of which displays distinct catalytic as well as noncatalytic binding properties: the cytosolic enzymes are encoded by at
Melissa P Mezzari et al.
Plant physiology, 138(2), 858-869 (2005-06-01)
Understanding the function of detoxifying enzymes in plants toward xenobiotics is of major importance for phytoremediation applications. In this work, Arabidopsis (Arabidopsis thaliana; ecotype Columbia) seedlings were exposed to 0.6 mm acetochlor (AOC), 2 mm metolachlor (MOC), 0.6 mm 2,4,6-trinitrotoluene

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