You Searched For: Iron+(III)+sulphate+hydrate

Catalog Number: (BOSSBS-12448R-A555)

Supplier: Bioss

Description: The alcohol dehydrogenase family of proteins metabolize a wide variety of substrates, including retinol, hydroxysteroids, ethanol, aliphatic alcohols and lipid peroxidation products. ADH5 (alcohol dehydrogenase 5 (class III)), also known as FDH (formaldehyde dehydrogenase), ADHX, ADH-3 or GSNOR, is a 374 amino acid cytoplasmic protein that belongs to the class III subfamily of alcohol dehydrogenases. Expressed ubiquitously, ADH5 uses iron as a cofactor to catalytically oxidize both long-chain primary alcohols and S-hydroxymethyl-glutathione, a product formed spontaneously between formaldehyde and glutathione. ADH5 exists as a homodimer and, via its ability to oxidize S-hydroxymethyl-glutathione and, thus, eliminate formaldehyde, functions as an important component of cellular metabolism. Genetic variations in the gene encoding ADH5 may affect drug and alcohol dependence in humans.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-12448R-FITC)

Supplier: Bioss

Description: The alcohol dehydrogenase family of proteins metabolize a wide variety of substrates, including retinol, hydroxysteroids, ethanol, aliphatic alcohols and lipid peroxidation products. ADH5 (alcohol dehydrogenase 5 (class III)), also known as FDH (formaldehyde dehydrogenase), ADHX, ADH-3 or GSNOR, is a 374 amino acid cytoplasmic protein that belongs to the class III subfamily of alcohol dehydrogenases. Expressed ubiquitously, ADH5 uses iron as a cofactor to catalytically oxidize both long-chain primary alcohols and S-hydroxymethyl-glutathione, a product formed spontaneously between formaldehyde and glutathione. ADH5 exists as a homodimer and, via its ability to oxidize S-hydroxymethyl-glutathione and, thus, eliminate formaldehyde, functions as an important component of cellular metabolism. Genetic variations in the gene encoding ADH5 may affect drug and alcohol dependence in humans.

UOM: 1 * 100 µl

Supplier: Alfa Aesar

Description: Terbium(III) chloride hexahydrate ≥99.9% (REO, rare earth oxide basis), REacton®

Catalog Number: (ACRO454110010)

Supplier: Thermo Scientific

Description: Bismuth(III) nitrate pentahydrate 98%, pure

UOM: 1 * 1 kg

Supplier: Alfa Aesar

Description: Europium trinitrate hydrate ≥99.99% (REO, rare earth oxide basis), REacton®

MSDS Certificates

Supplier: Alfa Aesar

Description: Yttrium(III) bromide, hydrate ≥99.99% (REO, rare earth oxide basis), REacton®

Supplier: Alfa Aesar

Description: Potassium aquapentachlororuthenate(III) (≥26,4% Ru) ≥99.99% (metals basis), Premion®

Catalog Number: (APOSIN3595-2G)

Supplier: APOLLO SCIENTIFIC

Description: Dithulium tricarbonate hydrate 99,9%

UOM: 1 * 2 g

Supplier: Thermo Scientific

Description: Ytterbium(III) chloride hexahydrate 99.99+% (trace metals basis)

MSDS

Supplier: Alfa Aesar

Description: Holmium tribromide hydrate ≥99.99% (REO, rare earth oxide basis), REacton®

Supplier: Alfa Aesar

Description: Scandium(III) chloride hexahydrate ≥99.99% (REO, rare earth oxide basis), REacton®

Supplier: Alfa Aesar

Description: Dysprosium trichloride hydrate ≥99.9% (REO, rare earth oxide basis)

Supplier: Alfa Aesar

Description: Terbium(III) chloride hexahydrate ≥99.99% (REO, rare earth oxide basis), REacton®

Supplier: Alfa Aesar

Description: Dysprosium trichloride hydrate ≥99.99% (REO, rare earth oxide basis)

Catalog Number: (BOSSBS-12448R-A680)

Supplier: Bioss

Description: The alcohol dehydrogenase family of proteins metabolize a wide variety of substrates, including retinol, hydroxysteroids, ethanol, aliphatic alcohols and lipid peroxidation products. ADH5 (alcohol dehydrogenase 5 (class III)), also known as FDH (formaldehyde dehydrogenase), ADHX, ADH-3 or GSNOR, is a 374 amino acid cytoplasmic protein that belongs to the class III subfamily of alcohol dehydrogenases. Expressed ubiquitously, ADH5 uses iron as a cofactor to catalytically oxidize both long-chain primary alcohols and S-hydroxymethyl-glutathione, a product formed spontaneously between formaldehyde and glutathione. ADH5 exists as a homodimer and, via its ability to oxidize S-hydroxymethyl-glutathione and, thus, eliminate formaldehyde, functions as an important component of cellular metabolism. Genetic variations in the gene encoding ADH5 may affect drug and alcohol dependence in humans.

UOM: 1 * 100 µl

Supplier: APOLLO SCIENTIFIC

Description: Aluminium nitrate hydrate 99,9%