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G6511

Sigma-Aldrich

Glutathione S-Transferase from equine liver

lyophilized powder, ≥25 units/mg protein

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Sinónimos:
GST, Glutathione R-transferase, Glutathione S-alkenetransferase, Glutathione S-alkyltransferase, Glutathione S-aralkyltransferase, Glutathione S-aryltransferase, Glutathione S-epoxidetransferase
Número de CAS:
50812-37-8
Comisión internacional de enzimas:
2.5.1.18 (BRENDA, IUBMB)
Número MDL:
MFCD00131198
NACRES:
NA.47

origen biológico

equine liver

Nivel de calidad

200

formulario

lyophilized powder

specific activity

≥25 units/mg protein

mol peso

45-50 kDa

composición

Protein, ≥60%

temp. de almacenamiento

−20°C

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Este artículo
GS52GS38GS90
Sigma-Aldrich

Sigma-Aldrich

G6511

Glutathione S-Transferase from equine liver

Sigma-Aldrich

Sigma-Aldrich

GS52

GST T2-2, Recombinant Human

Sigma-Aldrich

Sigma-Aldrich

GS38

GST T1-1, Recombinant Rat

Sigma-Aldrich

Sigma-Aldrich

GS90

GST T1-1, Recombinant Human

form

lyophilized powder

form

frozen liquid

form

frozen liquid

form

frozen liquid

mol wt

45-50 kDa

mol wt

25 kDa

mol wt

25 kDa

mol wt

25 kDa

storage temp.

−20°C

storage temp.

−70°C

storage temp.

−70°C

storage temp.

−70°C

specific activity

≥25 units/mg protein

specific activity

12.6 units/mg protein (as assayed by the spectrophotometric determination of NADPH oxidation coupled to the glutathione peroxidase activity of GST T2-2 on cumene hydroperoxide (1.5 mM) in the presence of reduced glutathione (1 mM) in 100 mM NaPO4 (pH 7.0) at room temperature.)

specific activity

86.6 (using spectrophotometric determination of 1,2-epoxy-3(4-nitrophenoxy)propane (ENPP) conjugation with reduced glutathione (5 mM) in 100 mM NaPO4 (pH 6.5) at room temperature.)

specific activity

8.8 units/mg protein (as assayed by the spectrophotometric determination of NADPH oxidation coupled to the glutathione peroxidase activity of GST T1-1 on cumene hydroperoxide (1.5 mM) in the presence of reduced glutathione (1 mM) in 100 mM NaPO4 (pH 7.0) at room temperature.)

composition

Protein, ≥60%

composition

-

composition

-

composition

-

Descripción general

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.

Acciones bioquímicas o fisiológicas

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.

Definición de unidad

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.

Forma física

Lyophilized powder containing Tris, reduced glutathione and EDTA.

Nota de análisis

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.

inhibidor

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Código de clase de almacenamiento

11 - Combustible Solids

WGK

WGK 3

Punto de inflamabilidad F

Not applicable

Punto de inflamabilidad C

Not applicable

Equipo de protección personal

Eyeshields, Gloves, type N95 (US)

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T1503
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25G
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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
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
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)
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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