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G6137

Sigma-Aldrich

Glutathione Peroxidase from bovine erythrocytes

lyophilized powder, ≥300 units/mg protein

Sinónimos:

GSH-Px, Glutathione:hydrogen-peroxide oxido-reductase

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About This Item

Número de CAS:
9013-66-5
Comisión internacional de enzimas:
1.11.1.9 (BRENDA, IUBMB)
Número CE:
232-749-6
Número MDL:
MFCD00131195
Código UNSPSC:
12352204
NACRES:
NA.54

origen biológico

bovine erythrocytes

Nivel de calidad

200

Formulario

lyophilized powder

actividad específica

≥300 units/mg protein

mol peso

84.5 kDa

composición

Protein, 10-30% modified Warburg-Christian

Condiciones de envío

dry ice

temp. de almacenamiento

−20°C

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Descripción general

Glutathione peroxidase is an antioxidant enzyme that contains selenium. It is present in the glandular epithelium of human endometrium.

Aplicación

Glutathione Peroxidase from bovine erythrocytes has been used as an oxygen radical scavenger to study its effect on cytotoxicity of 1,3-dilinoleoylglycerol (DLG) against E1A-3Y1 cells.
Glutathione peroxidase from bovine erythrocytes was used as a positive control in cloning and characterization of full-length cDNAs encoding two glutathione peroxidases (GpXs) from Globodera rostochiensis. It was used for the determination of glutathione peroxidase activity in human milk.

Acciones bioquímicas o fisiológicas

Glutathione peroxidase helps to reduce (peroxides) H2O2 to water and lipid peroxides to lipid alcohols.
Glutathione peroxidase is an enzyme which reduced lipid hydroperoxides into their corresponding alcohols. It also reduces free hydrogen peroxide in to water. In vivo it is responsible for protecting hemoglobin from oxidative breakdown.
Protects cells against oxidative damage by catalyzing the reduction of hydrogen peroxide in the presence of reducing agent glutathione. In cellular membranes it may induce lipid peroxidation through the reduction of hydrogen peroxide or polyunsaturated fatty acid hydroperoxides.

Definición de unidad

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.

Forma física

Lyophilized powder containing 25% sucrose and 2.5% dithiothreitol with sodium phosphate buffer salts

Otras notas

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.

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Referencia del producto
Descripción
Precios

Pictogramas

Health hazard
GHS08

Palabra de señalización

Danger

Frases de peligro

H334

Consejos de prudencia

P261 - P284 - P501

Clasificaciones de peligro

Resp. Sens. 1

Código de clase de almacenamiento

11 - Combustible Solids

Clase de riesgo para el agua (WGK)

WGK 3

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable

Equipo de protección personal

Eyeshields, Gloves, type N95 (US)

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Certificados de análisis (COA)

Lot/Batch Number
0000387803
0000387803
0000369501
0000342737
0000342736

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Superóxido dismutasa from bovine erythrocytes lyophilized powder, ≥3,000 units/mg protein, Protein ≥95 % by biuret

Sigma-Aldrich

S7571

Superóxido dismutasa from bovine erythrocytes

Cumene hydroperoxide technical grade, 80%

Sigma-Aldrich

247502

Cumene hydroperoxide

J T Jones et al.
Gene, 324, 47-54 (2003-12-25)
We report the cloning and characterisation of full-length DNAs complementary to RNA (cDNAs) encoding two glutathione peroxidases (GpXs) from a plant parasitic nematode, the potato cyst nematode (PCN) Globodera rostochiensis. One protein has a functional signal peptide that targets the
Angeles Torres et al.
Die Nahrung, 47(6), 430-433 (2004-01-20)
An analytical method for determining glutathione peroxidase (GPx) (EC 1.11.1.9) activity in whole blood has been adapted to human milk samples. The values obtained for precision (relative standard deviation: 8.4%), linearity and accuracy (recovery: 90.4%) indicate the adequacy of the
The role of oxidative stress in endometriosis
Handbook of Fertility, 273-281 (2015)
Reactive oxygen species, oxidative stress, and vascular biology in hypertension
Comprehensive hypertension, 337-344 (2007)
Yue Wang et al.
Analytical chemistry, 92(2), 1997-2004 (2019-12-21)
Solid evidence confirms that glutathione peroxidase (GPx) is a kind of vital protease in the first-line antioxidant defense system and participates in regulation of redox homeostasis as well as the pentose phosphate pathway. However, the current methods cannot achieve real-time
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