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G6511

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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Size/SKUAvailabilityPrice
1 mg

Estimated to ship onOctober 19, 2026fromMILWAUKEE

$50.50
5 mg

Available to ship TODAYfromMILWAUKEE

$157.00
10 mg

Available to ship TODAYfromMILWAUKEE

$259.00
25 mg

Estimated to ship onOctober 19, 2026fromMILWAUKEE

$540.00

About This Item

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

$50.50


Estimated to ship onOctober 19, 2026Details


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biological 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.

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.

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This Item
A7340GS90GS52
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

human

Quality Level

200

Quality Level

200

Quality Level

-

Quality Level

-

form

lyophilized powder

form

buffered aqueous solution

form

frozen liquid

form

frozen liquid

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−70°C

storage temp.

−70°C

mol wt

45-50 kDa

mol wt

antigen 27.5 kDa

mol wt

25 kDa

mol wt

25 kDa

specific activity

≥25 units/mg protein

specific activity

-

specific activity

8.8 units/mg protein

specific activity

12.6 units/mg protein


Pictograms

Health hazard

Signal Word

Danger

Hazard Codes

Precautionary Statements

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

WGK

WGK 1

Flash Point (°F)

Not applicable

Flash Point (°C)

Not applicable

PPE (personal protective equipment)

Eyeshields, Gloves, type N95 (US)



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