55689
Alcohol Dehydrogenase equine
recombinant, expressed in E. coli, ≥0.5 U/mg
Synonim(y):
ADH
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Wybierz wielkość
100 MG
893,00 zł
500 MG
3170,00 zł
893,00 zł
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Informacje o tej pozycji
Numer 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
Przejdź do
Pomoc techniczna
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Pozwól nam pomócbiological source
equine
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
Quality Level
Gene Information
equine ... ADH1(111772995)
1 of 4
Ta pozycja | 74931 | A8656 | A7011 |
|---|---|---|---|
| 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.[1]
Alcohol dehydrogenase is a zinc metalloprotein that forms five classes of isoenzymes through the dimerization of eight different subunits.[1]
Application
Alcohol Dehydrogenase equine has been used in in vitro alcohol dehydrogenase (Adh) assay.[2]
Biochem/physiol Actions
Alcohol dehydrogenase catalyzes the oxidative conversion of alcohol into aldehyde[3]. 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.[4] Binding of NAD+ in the active site[5] causes conformational changes which create the binding site for the alcohol substrate. [6]
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.[7] Moreover, alcohol dehydrogenase can oxidize ethanol while simultaneously reducing nicotinamide adenine dinucleotide (NAD+) to NADH.[1] 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.[8]
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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signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Klasa składowania
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.
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
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)
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)
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