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G4013
Glutathione Peroxidase from human erythrocytes
lyophilized powder, ≥30 units/mg protein
Synonym(s):
GSH-Px, Glutathione:hydrogen-peroxide oxido-reductase
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About This Item
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lyophilized powder
specific activity
≥30 units/mg protein
composition
Protein, 13-25% modified Warburg-Christian
UniProt accession no.
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.[1]
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).[1]
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.[1]
Physical form
Lyophilized powder containing 25% sucrose, 3% dithiothreitol, and sodium phosphate buffer salts
Other Notes
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.
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
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Jennifer Walshe et al.
Cancer research, 67(10), 4751-4758 (2007-05-19)
Cutaneous squamous cell carcinomas (CSCC) are a common malignancy of keratinocytes that arise in sites of the skin exposed to excessive UV radiation. In the present study, we show that human SCC cell lines, preneoplastic solar keratoses (SK), and CSCC
Tengku Ahbrizal Farizal Tengku Ahmad et al.
Molecules (Basel, Switzerland), 18(2), 2200-2211 (2013-02-26)
The present study was designed to determine the radioprotective effects of Malaysian Gelam honey on gene expression and enzyme activity of superoxide dismutase (SOD), catalase (CAT) and glutathione peroxidase (GPx) of human diploid fibroblasts (HDFs) subjected to gamma-irradiation. Six groups
O L Gostukhina et al.
Zhurnal evoliutsionnoi biokhimii i fiziologii, 48(6), 542-547 (2013-02-14)
The work studied the content of carotinoids, the state of antioxidant (AO) enzymatic complex, and intensity of lipid peroxidation in tissues (hepatopancreas, gill, foot) of the Black Sea bivalve mollusc Anadara inaequivalvis. Tissues with a high content of the pigment
Hai-Dong Yao et al.
The Journal of nutrition, 143(5), 613-619 (2013-03-22)
Dietary selenium (Se) deficiency causes muscular dystrophy in various species, but the molecular mechanism remains unclear. Our objectives were to investigate: 1) if dietary Se deficiency induced different amounts of oxidative stress, lipid peroxidation, and cell apoptosis in 3 skeletal
Bing-Lin Zhang et al.
Environmental toxicology and chemistry, 32(6), 1420-1425 (2013-02-19)
The effect of sodium chloride (NaCl) on cadmium (Cd) uptake, translocation, and oxidative stress was investigated using 2 tobacco cultivars differing in Cd tolerance. The growth inhibition of the tobacco plants exposed to Cd toxicity was in part alleviated by
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Do you have any solution stability information on glutathione peroxidase from erythrocytes?
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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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