U heeft gezocht op: 2-Chloro-5-iodobenzyl+alcohol


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Leverancier: VWR Collection
Omschrijving: Deze veiligheidssuikerweegschaal gecombineerd met thermo-hydrometers kan het soortelijk gewicht, Brix en alcohol per volume bepalen.

Catalogus nummer: (325351000.)
Leverancier: Thermo Fisher Scientific
Omschrijving: Methanol-D4 (99.8% D) + 0.03% (v/v) TMS, AcroSeal® for NMR spectroscopy
UOM: 1 * 100 mL

MSDS


Leverancier: Merck
Omschrijving: 4-Hydroxy-4-methyl-2-pentanon for synthesis, Sigma-Aldrich®
Leverancier: Thermo Fisher Scientific
Omschrijving: (±)-Tetrahydro-2-furfurylmethanol 99+%
Leverancier: TCI
Omschrijving: (±)-1-Phenyl-1-propanol ≥98.0% (by GC)

Leverancier: Avantor
Omschrijving: 1,2-Ethaandiol ≥99.0% (by GC), BAKER ANALYZED®, J.T.Baker®
Leverancier: Thermo Fisher Scientific
Omschrijving: Slightly soluble in water, soluble in conc. H₂SO₄. Insoluble in alcohol
Leverancier: Merck
Omschrijving: Organic Standard, Ethanol-150, 10× Ampoule of 1,2 ml, Verpakking: Ampoule

Leverancier: Thermo Fisher Scientific
Omschrijving: 2-(4-Fluorophenyl)ethanol ≥97%
Catalogus nummer: (BOSSBS-12448R-FITC)
Leverancier: Bioss
Omschrijving: 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


Catalogus nummer: (BOSSBS-12448R-A555)
Leverancier: Bioss
Omschrijving: 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


Leverancier: Apollo Scientific
Omschrijving: Under Mitsunobu conditions primary and secondary alcohols can be protected as hexafluorophenylisopropyl(HIP) ethers: J. Am. Chem. Soc., 116, 8354 (1994).

Leverancier: TCI
Omschrijving: Furfurylalcohol ≥98.0% (by GC)

Leverancier: Thermo Fisher Scientific
Omschrijving: 2-Phenyl-2-propanol ≥98%
Leverancier: Apollo Scientific
Omschrijving: 2-(4-Nitrophenyl)ethanol 98%

Leverancier: Thermo Fisher Scientific
Omschrijving: 2-(4-Aminophenyl)ethanol 97%
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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 at 1-800-932-5000.
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 Regulatory_Affairs@vwr.com
-Additional Documentation May be needed to purchase this item. A VWR representative will contact you if needed.
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