G6511
Glutathione S-Transferase from equine liver
lyophilized powder, ≥25 units/mg protein
Sinónimos:
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
Número de CAS:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.47
Productos recomendados
biological source
equine liver
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.
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
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Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
11 - Combustible Solids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Los clientes también vieron
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)
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
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
Piotr Jakubowski et al.
Toxicology and applied pharmacology, 269(1), 34-42 (2013-03-19)
Snake venom antagonists of α2β1 integrin have been identified as members of a C-lectin type family of proteins (CLP). In the present study, we characterized three new CLPs isolated from Echis sochureki venom, which interact with this integrin. These proteins
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