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G6137

Glutathione Peroxidase from bovine erythrocytes

Name: Glutathione Peroxidase from bovine erythrocytes
Brand: SIGMA

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)

EC Number:

232-749-6

MDL number:

MFCD00131195

UNSPSC Code:

12352204

NACRES:

NA.54

biological source

bovine erythrocytes

Quality Level

200

form

lyophilized powder

specific activity

≥300 units/mg protein

mol wt

84.5 kDa

composition

Protein, 10-30% modified Warburg-Christian

shipped in

dry ice

storage temp.

−20°C

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General description

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

Application

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.

Biochem/physiol Actions

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.

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 and 2.5% dithiothreitol with sodium phosphate buffer salts

Other Notes

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.

pictograms

GHS08

signalword

Danger

hcodes

H334

pcodes

P261 - P284 - P501

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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Sigma-Aldrich

247502

Cumene hydroperoxide

Glutathione Peroxidase-Activatable Two-Photon Ratiometric Fluorescent Probe for Redox Mechanism Research in Aging and Mercury Exposure Mice Models.

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

Hemoglobin catabolism. I. Glutathione peroxidase, an erythrocyte enzyme which protects hemoglobin from oxidative breakdown.

G C MILLS

The Journal of biological chemistry, 229(1), 189-197 (1957-11-01)

Selenium-dependent peroxidases suppress 5-lipoxygenase activity in B-lymphocytes and immature myeloid cells. The presence of peroxidase-insensitive 5-lipoxygenase activity in differentiated myeloid cells.

O Werz et al.

European journal of biochemistry, 242(1), 90-97 (1996-11-15)

Differentiation of HL-60 cells by dimethylsulfoxide induces 5-lipoxygenase protein expression, but only low cellular 5-lipoxygenase activity. Similarly, B-lymphocytes express 5-lipoxygenase protein and show activity in cell homogenates but not in intact cells. Here, we demonstrate that suppression of cellular 5-lipoxygenase

The role of oxidative stress in endometriosis

Handbook of Fertility, 273-281 (2015)

Determination of glutathione peroxidase activity in human milk.

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

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