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55689

Alkoholdehydrogenase equine

recombinant, expressed in E. coli, ≥0.5 U/mg

Synonym(e):

ADH

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€ 169,00

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€ 671,00

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Über diesen Artikel

CAS-Nummer:
9031-72-5
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-870-4
MDL number:
MFCD00081305
EG-Nummer:
1.1.1.1 (BRENDA, IUBMB)
Specific activity:
≥0.5 U/mg
Biological source:
equine
Recombinant:
expressed in E. coli

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Unterstützung erhalten

biological source

equine

Quality Level

100

recombinant

expressed in E. coli

description

Isozyme E sequence

form

lyophilized powder

specific activity

≥0.5 U/mg

color

white, light yellow

pH

7

solubility

water: 5 mg/mL

application(s)

life science and biopharma

storage temp.

−20°C

Gene Information

equine ... ADH1(111772995)

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Dieser Artikel
74931A8656A7011
Alcohol Dehydrogenase equine recombinant, expressed in E. coli, ≥0.5 U/mg

Sigma-Aldrich

55689

Alcohol Dehydrogenase equine

Alcohol Dehydrogenase ≥10.0 U/mg

Sigma-Aldrich

74931

Alcohol Dehydrogenase

Alcohol Dehydrogenase from Saccharomyces cerevisiae

Sigma-Aldrich

A8656

Alcohol Dehydrogenase from Saccharomyces cerevisiae

Alcohol Dehydrogenase from Saccharomyces cerevisiae ≥300 units/mg protein, lyophilized powder (contains buffer salts), Mw 141-151 kDa

Sigma-Aldrich

A7011

Alcohol Dehydrogenase from Saccharomyces cerevisiae

Gene Information

equine ... ADH1(111772995)

Gene Information

-

Gene Information

-

Gene Information

-

biological source

equine

biological source

-

biological source

Saccharomyces cerevisiae

biological source

Saccharomyces cerevisiae

specific activity

≥0.5 U/mg

specific activity

≥10.0 U/mg

specific activity

-

specific activity

≥300 units/mg protein

application(s)

life science and biopharma

application(s)

-

application(s)

-

application(s)

diagnostic assay manufacturing

recombinant

expressed in E. coli

recombinant

-

recombinant

-

recombinant

-

form

lyophilized powder

form

powder

form

powder

form

lyophilized powder (contains buffer salts)

General description

Research Area: Neuroscience
Alcohol dehydrogenase is a zinc metalloprotein that forms five classes of isoenzymes through the dimerization of eight different subunits.

Application

Alcohol Dehydrogenase equine has been used in in vitro alcohol dehydrogenase (Adh) assay.

Biochem/physiol Actions

Alcohol dehydrogenase catalyzes the oxidative conversion of alcohol into aldehyde[1]. It has a homodimeric structure with a co-enzyme binding domain at the C-terminal and an N-terminal catalytic domain. The active site is located at the interdomain cleft.[2] Binding of NAD+ in the active site[3] causes conformational changes which create the binding site for the alcohol substrate. [4]
Horse liver alcohol dehydrogenase (HL-ADH) is an enzyme with broad specificity, capable of catalyzing the reversible oxidation of a wide variety of primary and secondary alcohols to form their corresponding aldehydes and ketones. Moreover, alcohol dehydrogenase can oxidize ethanol while simultaneously reducing nicotinamide adenine dinucleotide (NAD+) to NADH. Previous studies have demonstrated that ADH and ALDH variants can influence alcohol dependence. Additionally, the ADH genotype has been linked to lacunar infarction and neuropsychiatric diseases.

Other Notes

1 U corresponds to the amount of enzyme which reduces 1 μmol benzaldehyde per minute at pH 7.0 and 30 °C.

pictograms

Health hazard
GHS08

signalword

Danger

hcodes

H334

Hazard Classifications

Resp. Sens. 1

Lagerklasse

11 - Combustible Solids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

Hier finden Sie alle aktuellen Versionen:

Analysenzertifikate (COA)

Lot/Batch Number
BCCN7571
BCCM3119
BCCK5048
BCCH6411
BCCD2440

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Wenn Sie eine bestimmte Version benötigen, können Sie anhand der Lot- oder Chargennummer nach einem spezifischen Zertifikat suchen.

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Die Dokumentenbibliothek aufrufen

Ioanna A Gorbunova et al.
The journal of physical chemistry. B, 125(34), 9692-9707 (2021-08-20)
The dynamics of polarized fluorescence in NADH in alcohol dehydrogenase (ADH) in buffer solution has been studied using the TCSPC spectroscopy. A global fit procedure was used for determination of the fluorescence parameters from experiment. The interpretation of the results
In vitro activation of NAD-dependent alcohol dehydrogenases by Nudix hydrolases is more widespread than assumed
Ochsner AM, et al.
Febs Letters, 588(17), 2993-2999 (2014)
Horse Liver Alcohol Dehydrogenase-Catalyzed Aldehyde Oxidation
Oppenheimer NJ and Henehan G TM
The Journal of Biological Chemistry, 407-415 (1995)
Ethanol metabolism and implications for disease
Rajendram R, et al.
Neuropathology of Drug Addictions and Substance Misuse, 377-388 (2016)
Association study of alcohol dehydrogenase and aldehyde dehydrogenase polymorphism with Alzheimer disease in the Taiwanese population
Wu YY, et al.
Frontiers in Neuroscience, 15, 625885-625885 (2021)
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Global Trade Item Number

SKUGTIN
55689-100MG04061833228135
55689-500MG04061833228142

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