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G4013

Sigma-Aldrich

Glutathione Peroxidase from human erythrocytes

lyophilized powder, ≥30 units/mg protein

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Synonym(s):
GSH-Px, Glutathione:hydrogen-peroxide oxido-reductase
CAS Number:
9013-66-5
Enzyme Commission number:
1.11.1.9 (BRENDA, IUBMB)
MDL number:
MFCD00131195
UNSPSC Code:
12352204

form

lyophilized powder

specific activity

≥30 units/mg protein

composition

Protein, 13-25% modified Warburg-Christian

UniProt accession no.

P07203

shipped in

dry ice

storage temp.

−20°C

Gene Information

human ... GPX1(2876)

General description

GPX1 (glutathione peroxidase 1) belongs to the four membered family of GPXs, including GPX2, GPX3 and GPX4. It is a selenocysteine-containing protein. GPX1 is the major isoform of GPX enzyme and is ubiquitously present intracellularly.
Note: At the reported pH optimum of 8.8, we have found the activity to be approx. 10 times that at pH 7.0. However, to remain consistent with literature and avoid complications arising from non-enzymatic oxidation of GSH, our unit is defined at pH 7.0.

Application

Glutathione peroxidase (GPX) from human erythrocytes has been used for the determination of the ability of peroxides to inactivate GPX in epithelial sheets obtained from cutaneous squamous cell carcinoma (CSCC) or solar keratoses (SK).

Biochem/physiol Actions

GPX1 (glutathione peroxidase 1) catalyzes the conversion of multiple organic and inorganic peroxides, by utilizing reduced glutathione (GSH) as an electron donor. This enzyme is also responsible for the removal of organic and inorganic peroxides.

Unit Definition

One unit will catalyze the oxidation by H2O2 of 1.0 μmole of reduced glutathione to oxidized glutathione per min at pH 7.0 at 25 °C.

Physical form

Lyophilized powder containing 25% sucrose, 3% dithiothreitol, and sodium phosphate buffer salts

Pictograms

Health hazard
GHS08

Signal Word

Danger

Hazard Statements

H334

Hazard Classifications

Resp. Sens. 1

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

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  1. Which document(s) contains shelf-life or expiration date information for a given product?

    If available for a given product, the recommended re-test date or the expiration date can be found on the Certificate of Analysis.

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    Transportation information can be found in Section 14 of the product's (M)SDS.To access the shipping information for this material, use the link on the product detail page for the product. 

  5. Do you have any solution stability information on glutathione peroxidase from erythrocytes?

    The following information on the bovine source enzyme (equivalent to Product G6137) probably also applies to the human source enzyme (G4013). According to the literature, there is no appreciable loss after 3 months in the presence of 1 mM dithiothreitol (DTT) if solutions of the enzyme are frozen. There is a significant loss (15-22%) in 1 month when in the presence of 2 mM reduced glutathione (GSH), and if neither DTT nor GSH present, the loss is even greater (60-70% lost in 1 month frozen.1There are also stability concerns with the powdered form of Glutathione Peroxidase; the powder is shipped on dry ice and should be kept frozen. We have found that the powder should be stable at least a year if stored in the freezer below 0°C.In our experience, without DTT or mercaptoethanol present, a solution of Glutathione Peroxidase may lose much of its activity within a day, even on ice. Our general recommendation is to reconstitute in 10 mM sodium phosphate, pH 7.0 with at least 1 mM dithiothreitol. The solution should be divided into working aliquots and promptly frozen; it will be stable through one freeze-thaw cycle.1. Biochimica et Biophysica Acta, 358, 251-261 (1974).

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