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| Ihnen/SKU | Verfügbarkeit | Preis |
|---|---|---|
1 mg | Warenkorb auf Verfügbarkeit prüfen | € 39,50 |
5 mg | Warenkorb auf Verfügbarkeit prüfen | € 114,00 |
10 mg | Warenkorb auf Verfügbarkeit prüfen | € 199,00 |
25 mg | Warenkorb auf Verfügbarkeit prüfen | € 398,00 |
Über diesen Artikel
CAS-Nummer:
UNSPSC Code:
12352204
NACRES:
NA.47
MDL number:
Technischer Dienst
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Unterstützung erhaltenbiological source
equine liver
Quality Segment
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.
Protein family catalyzing conjugation of reduced glutathione with various hydrophobic chemicals.
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.
Other Notes
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.
1 of 1
Dieser Artikel | |||
|---|---|---|---|
| description lyophilized powder, ≥25 units/mg protein | description IgG fraction of antiserum, buffered aqueous solution | description - | description - |
| biological source equine liver | biological source rabbit | biological source human | biological source rat |
| Quality Level 200 | Quality Level 200 | Quality Level 100 | Quality Level 100 |
| form lyophilized powder | form buffered aqueous solution | form frozen liquid | form frozen liquid |
| mol wt 45-50 kDa | mol wt antigen 27.5 kDa | mol wt 25 kDa | mol wt 25 kDa |
| storage temp. −20°C | storage temp. −20°C | storage temp. −70°C | storage temp. −70°C |
| composition Protein, ≥60% | composition - | composition - | composition - |
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Lagerklasse
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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