16892
Alcohol Dehydrogenase
≥10,000 units/mL
Synonym(s):
ADH
recombinant
expressed in E. coli
form
liquid
specific activity
≥10,000 units/mL
storage temp.
−20°C
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Preparation Note
The original source organism of the sequence of this ADH is proprietary information.
Other Notes
One unit corresponds to the amount of enzyme which reduces 1 μmole ethyl-2-oxo-4-phenylbutyrate per minute at pH 7.0 and 37 °C
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
Storage Class Code
11 - Combustible Solids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
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Xingxing Diao et al.
Drug metabolism and disposition: the biological fate of chemicals, 41(2), 430-444 (2012-11-22)
3-n-Butylphthalide (NBP) is a cardiovascular drug currently used for the treatment of cerebral ischemia. The present study aims to investigate the metabolism, pharmacokinetics, and excretion of NBP in humans and identify the enzymes responsible for the formation of major metabolites.
Kate M Ehrensberger et al.
The Journal of biological chemistry, 288(2), 759-769 (2012-12-12)
In yeast, Adh1 (alcohol dehydrogenase 1) is an abundant zinc-binding protein that is required for the conversion of acetaldehyde to ethanol. Through transcriptome profiling of the Schizosaccharomyces pombe genome, we identified a natural antisense transcript at the adh1 locus that
Nathan C Contino et al.
Journal of the American Society for Mass Spectrometry, 24(1), 101-108 (2012-12-01)
Charge detection mass spectrometry (CDMS) measurements have been performed for cytochrome c and alcohol dehydrogenase (ADH) monomer using a modified cone trap incorporating a cryogenically cooled JFET. Cooling the JFET increases its transconductance and lowers thermal noise, improving the signal
Shuo Zhou et al.
Biotechnology letters, 35(3), 359-365 (2012-11-20)
The gene encoding a novel short-chain alcohol dehydrogenase in the thermophilic bacterium, Carboxydothermus hydrogenoformans, was identified and overexpressed in Escherichia coli. The enzyme was thermally stable and displayed the highest activity at 70 °C and pH 6.0. It preferred NAD(H) over
Liron Amir et al.
Journal of the American Chemical Society, 135(1), 70-73 (2012-12-13)
The generation of a current through interaction between bacteria and electrodes has been explored by various methods. We demonstrate the attachment of living bacteria through a surface displayed redox enzyme, alcohol dehydrogenase II. The unnatural amino acid para-azido-L-phenylalanine was incorporated
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