Skip to Content
Merck
All Photos(1)

Key Documents

View All Documentation

49854

Sigma-Aldrich

Alcohol Dehydrogenase, recombinant from E. coli

5.0-15.0 U/mg

Synonym(s):

Alcohol:NADP+ oxidoreductase

Sign Into View Organizational & Contract Pricing
All Photos(1)

About This Item

CAS Number:
9028-12-0
Enzyme Commission number:
1.1.1.2 (BRENDA, IUBMB)
EC Number:
232-823-8
MDL number:
MFCD00130451
UNSPSC Code:
12352204
NACRES:
NA.54

recombinant

expressed in E. coli

form

crystals
powder or crystals

specific activity

5.0-15.0 U/mg

solubility

50 mM phosphate buffer pH 7.0: 1 mg/mL, clear to faintly turbid, slightly yellow to deep brownish-yellow

storage temp.

−20°C

Looking for similar products? Visit Product Comparison Guide

Unit Definition

1 U corresponds to the amount of enzyme which reduces 1 μmol acetone per minute at pH 7.0 and 30°C (NADPH as cofactor)

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Alcohol dehydrogenase-catalyzed synthesis of enantiomerically pure d-lactones as versatile intermediates for natural product synthesis.
Fischer, T. and Pietruszka, J.
Advanced Synthesis & Catalysis, 354, 2521-2530 (2012)
Chemo-promiscuity of alcohol dehydrogenases: reduction of phenylacetaldoxime to the alcohol.
Ferreira-Silva, B., et al.
Tetrahedron, 66, 3410-3414 (2010)
Alexandra Lerchner et al.
Biotechnology and bioengineering, 110(11), 2803-2814 (2013-05-21)
The NADP⁺-dependent alcohol dehydrogenase from Ralstonia sp. (RasADH) belongs to the protein superfamily of short-chain dehydrogenases/reductases (SDRs). As an enzyme that accepts different types of substrates--including bulky-bulky as well as small-bulky secondary alcohols or ketones--with high stereoselectivity, it offers potential
Günter E Jeromin
Biotechnology letters, 31(11), 1717-1721 (2009-07-01)
A new immobilisate of alcohol dehydrogenase (ADH) is described in which all components for the reaction, i.e. enzyme, the coenzyme NADP(+), the buffer and other cofactors (trace elements), are immobilized together. It is an all-inclusive catalyst. The support is a

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service