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Catalog Number: (80137.)
Supplier: Biotium
Description: CF® dye labeled dextrans could be used as a fluorescent fluid-phase markers to study cell permeability, endocytosis, or mechanisms of biomolecular delivery. The dextran is 3,500 MW, and contains a formaldehyde-fixable free-amine group.
UOM: 1 * 1 mg


Catalog Number: (BOSSBS-12448R-CY7)
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: (22015.)
Supplier: Biotium
Description: Ready-to-use formaldehyde-based fixation buffer for immunofluorescence staining for microscopy or flow cytometry.
UOM: 1 * 100 mL

MSDS


Catalog Number: (8.00757.0250)
Supplier: Merck
Description: Diethyl sebacate for synthesis, Sigma-Aldrich®
UOM: 1 * 250 mL

MSDS


Supplier: Merck
Description: Diethyl oxalate for synthesis, Sigma-Aldrich®
Catalog Number: (BOSSBS-12448R)
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: Merck
Description: N,N-Diethyl-2-ethanolammoniumchloride for synthesis, Sigma-Aldrich®
Supplier: Biotium
Description: CF® dye labeled dextrans could be used as a fluorescent fluid-phase markers to study cell permeability, endocytosis, or mechanisms of biomolecular delivery. The dextran is 40,000 MW, and contains a formaldehyde-fixable free-amine group.

Supplier: Biotium
Description: Biotium’s CellBrite™ NIR Cytoplasmic Membrane Dyes are near-infrared lipophilic carbocyanine dyes for labeling cytoplasmic membranes in live or formaldehyde-fixed cells.
Supplier: Biotium
Description: CF® dye labeled dextrans could be used as a fluorescent fluid-phase markers to study cell permeability, endocytosis, or mechanisms of biomolecular delivery. The dextran is 150,000 MW, and contains a formaldehyde-fixable free-amine group.

Supplier: Merck
Description: Diethyl phthalate for synthesis
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


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-A750)
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: Merck
Description: <B>All Spectroquant® test kits</B> can be used with the <B>Prove</B> range of spectrophotometers and Nova 60/60A instruments. Tests can be used not only on photometers and spectrophotometer from Merck, but also on photometers and spectrophotometers from other suppliers (programming details available on request). <B>Spectroquant® cell test kits.</B>
Catalog Number: (BOSSBS-12448R-A350)
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


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Stock for this item is limited, but may be available in a warehouse close to you. Please make sure that you are logged in to the site so that available stock can be displayed. If the call is still displayed and you need assistance, please call us on +353 1 88 22222
This product is marked as restricted and can only be purchased by approved Shipping Accounts. If you need further assistance, email VWR Regulatory Department at eurega_services@eu.vwr.com
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The original product is no longer available. The replacement shown is available.
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