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  • A8435 - Alcohol Dehydrogenase, NADP+ dependent from Thermoanaerobium brockii

A8435 Sigma

Alcohol Dehydrogenase, NADP+ dependent from Thermoanaerobium brockii Green Alternative

lyophilized powder, 5-15 units/mg protein

Synonym: Alcohol:NADP+ oxidoreductase, TBADH



Related Categories 1.1.x.x Acting on hydroxyl groups, 1.x.x.x Oxidoreductases, Alcohol Metabolism, Application Index, Biochemicals and Reagents,
form   lyophilized powder
composition   Protein, ≥20% biuret
greener alternative product characteristics   Waste Prevention: Greener alternative product characteristics
Learn more about the Principles of Green Chemistry.
greener alternative category   Enabling
storage temp.   −20°C


Biochem/physiol Actions

An extremely thermostable enzyme with broad substrate specificity for alcohols, ketones and acetaldehyde.

Alcohol Dehydrogenase, from Thermoanaerobium brockii, is an extremely thermostable enzyme with broad substrate specificity for alcohols, ketones and acetaldehyde. Alcohol dehydrogenases (ADHs) are enzymes that catalyze the reversible conversion of ketone/aldehydes to the corresponding alcohols using a nicotinamide cofactor.

General description

Sigma Life Science is committed to bringing you Greener Alternative Products, which adhere to one or more of The 12 Principles of Greener Chemistry. This product has been enhanced for waste prevention when used in fuel cell research. For more information see the article in biofiles.

Unit Definition

One unit will oxidize 1.0 μmole of 2-propanol to acetone per min at pH 7.8 at 40 °C in the presence of NADP+.

Physical form

Contains phosphate buffer salts and dithioerythritol


Alcohol dehydrogenase may be used to synthesize enantiomerically pure stereoisomers of chiral alcohols. It may be used to study ethanol fuel cells, alcoholism and drug dependence. Product A8435 is NADP+ dependent and is obtained from Thermoanaerobium brockii. It contains phosphate buffer salts and dithioerythritol. The product has been assayed with 2-propanol and NADP+ to analyse the function of fatty aldehyde reductase (FALDR) derived from Marinobacter aquaeolei VT8.

Price and Availability

All labs need water

Biomedical Applications
Safety & Documentation

Safety Information

NONH for all modes of transport
WGK Germany 
Protocols & Articles

Related Content

Enzymes & Proteins

Application Index | Enzyme Index | Substrate Index | Inhibitor Index | Cofactor Index | Lectin Index
Keywords: Cell signaling, Diagnostic, Drug discovery, Molecular biology

Peer-Reviewed Papers


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