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A6338

Aldehyd-Dehydrogenase, Kalium-aktiviert aus Backhefe (S. cerevisiae)

lyophilized powder, ≥2.0 units/mg protein

Synonym(e):

Aldehyd:NAD[P]+-Oxidoreduktase

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Ihnen/SKUVerfügbarkeitPreis
25 units
Warenkorb auf Verfügbarkeit prüfen
€ 65,40
100 units
Warenkorb auf Verfügbarkeit prüfen
€ 169,00
250 units
Warenkorb auf Verfügbarkeit prüfen
€ 345,00

Über diesen Artikel

CAS-Nummer:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-846-3
MDL number:
EG-Nummer:
Specific activity:
≥2.0 units/mg protein

€ 65,40


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form

lyophilized powder

Quality Segment

specific activity

≥2.0 units/mg protein

mol wt

228 kDa

composition

Protein, ≥5.0% biuret

shipped in

dry ice

storage temp.

−20°C

General description

Aldehyde dehydrogenase is a tetramer and has several different isoforms. The enzyme tested in 0.01 M pyrophosphate buffer shows a sharp optimum around pH 9.3 with acetaldehyde as substrate.[1] Potassium ions and cysteine are essential for the enzyme′s activity. Rubidium or NH4+ can be substituted for K+, and glutathione for cysteine. Lithium, Na+, and Cs+ inhibit the reaction.[2] Aldehyde dehydrogenase is inhibited by propylurea, crotonaldehyde, n-propyl isocyanate, cyclohexyl isocyanate, 1-n-propyl-1-[(4-chlorophenyl)sulphonyl]-3-n-propylurea, and 1-methyl-1-[(4-chlorophenyl)sulphonyl]-3-n-propylurea. The enzyme may be utilized to quantitate aldehydes present in blood.[3]
Aldehyde dehydrogenase (ALDH) is present in the nucleus, cytosol, mitochondria and endoplasmic reticulum of cells.

Application

Aldehyde dehydrogenase (ALDH) has been used to evaluate the effects of pear extracts on ALDH activity.[4] It has also been used to colorimetrically determine ethanol by monitoring the enzymatic reduction of nicotinamide adenine dinucleotide (NAD).

Biochem/physiol Actions

Aldehyde dehydrogenase from baker′s yeast catalyzes the reduction of pyridine nucleotides by several aldehydes.[2] It catalyzes the oxidation of a wide range of substrates, such as acetaldehyde, formaldehyde, propionaldehyde, n-butylaldehyde, isobutylaldehyde, n-valeraldehyde, caproaldehyde, benzaldehyde, glycoaldehyde, D-glyceraldehyde, malonic semialdehyde, and succinic aldehyde. Aldehyde dehydrogenase is used to study the production of ethanol and isobutanol.[5] Ethanol concentration can be determined colorimentrically by monitoring the enzymatic reduction of nicotinamide adenine dinucleotide (NAD) using alcohol dehydrogenase after preremoval of aldehyde by aldehyde dehydrogenase.[6][7]

Physical form

Enthält Trehalose, Kaliumphosphat und Citrat-Puffersalze, Dithiothreitol und Spuren von β-NAD und Propionsäure.

Preparation Note

This enzyme can be dissolved at 0.3 mg/mL in 100 mM Tris-HCl buffer (pH 8.0), containing 0.02% BSA.

Other Notes

1 U oxidiert 1.0 μmol Acetaldehyd zu Essigsäure pro Minute bei 25 °C und pH 8.0 in Anwesenheit von β-NAD+, Kalium und Thiolen.

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Dieser Artikel
A977010171832001126925
specific activity

≥2.0 units/mg protein

specific activity

≥10 units/mg protein

specific activity

~20 units/mg protein (At 25 °C with acetaldehyde as the substrate.)

specific activity

≥19 units/mg protein

form

lyophilized powder

form

lyophilized powder

form

lyophilized

form

lyophilized solid

shipped in

dry ice

shipped in

-

shipped in

-

shipped in

ambient

mol wt

228 kDa

mol wt

-

mol wt

-

mol wt

-

storage temp.

−20°C

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

Quality Level

200

Quality Level

200

Quality Level

-

Quality Level

100


Lagerklasse

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)



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Questions

  1. Re A6338...how was the enzyme purified, and is it confirmed to be free of other activities, e.g. alcohol dehydrogenase?

    1 answer
    1. The purification method is proprietary, and testing for other activities, such as alcohol dehydrogenase, is not conducted. The following reference from the Product Information Sheet may be helpful: Bostian, K. A., and Betts, G. F., Rapid purification and properties of potassium-activated aldehyde dehydrogenase from Saccharomyces cerevisiae. Biochemical Journal, 173(3), 773-786 (1978).

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