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Cambia visualizzazione
| Taglio della confezione | SKU | Disponibilità | Prezzo |
|---|---|---|---|
| 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:
Specific activity:
≥0.5 U/mg
Biological source:
equine
Recombinant:
expressed in E. coli
Servizio Tecnico
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Permettici di aiutartibiological 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.
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.
1 of 1
Questo articolo | |||
|---|---|---|---|
| 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 |
signalword
Danger
hcodes
pcodes
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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I documenti relativi ai prodotti acquistati recentemente sono disponibili nell’Archivio dei documenti.
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
| SKU | GTIN |
|---|---|
| 55689-100MG | 04061833228135 |
| 55689-500MG | 04061833228142 |




