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55689

Alcohol Dehydrogenase equine

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

Sinonimo/i:

ADH

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Taglio della confezioneSKUDisponibilitàPrezzo
100 mg
Per conoscere la disponibilità, visualizza il carrello
CHF 186.00
500 mg
Per conoscere la disponibilità, visualizza il carrello
CHF 717.00

Informazioni su questo articolo

Numero CAS:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-870-4
MDL number:
Numero CE:
Specific activity:
≥0.5 U/mg
Biological source:
equine
Recombinant:
expressed in E. coli

CHF 186.00


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biological source

equine

Quality Level

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)

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.

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Questo articolo
74931A8656A7011
specific activity

≥0.5 U/mg

specific activity

≥10.0 U/mg

specific activity

-

specific activity

≥300 units/mg protein

Gene Information

equine ... ADH1(111772995)

Gene Information

-

Gene Information

-

Gene Information

-

biological source

equine

biological source

-

biological source

Saccharomyces cerevisiae

biological source

Saccharomyces cerevisiae

recombinant

expressed in E. coli

recombinant

-

recombinant

-

recombinant

-

form

lyophilized powder

form

powder

form

powder

form

lyophilized powder (contains buffer salts)

application(s)

life science and biopharma

application(s)

-

application(s)

-

application(s)

diagnostic assay manufacturing


pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Classe di stoccaggio

11 - Combustible Solids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable



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Ethanol metabolism and implications for disease
Rajendram R, et al.
Neuropathology of Drug Addictions and Substance Misuse, 377-388 (2016)
Horse Liver Alcohol Dehydrogenase-Catalyzed Aldehyde Oxidation
Oppenheimer NJ and Henehan G TM
The Journal of Biological Chemistry, 407-415 (1995)
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)



Numero articolo commerciale globale

SKUGTIN
55689-100MG04061833228135
55689-500MG04061833228142

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