Skip to Content
MilliporeSigma

Skip To

A6338

Aldehyde Dehydrogenase, potassium-activated from baker′s yeast (S. cerevisiae)

lyophilized powder, ≥2.0 units/mg protein

Synonym(s):

Aldehyde:NAD[P]+ oxidoreductase

Sign In to View Organizational & Contract Pricing.

Select a Size

Change View
Size/SKUAvailabilityPrice
25 units
Check Cart for Availability
$84.20
100 units
Check Cart for Availability
$218.00
250 units
Check Cart for Availability
$448.00

About This Item

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

$84.20


Check Cart for Availability

​
Request a Custom Order
Technical Service
Need help? Our team of experienced scientists is here for you.
Let Us Assist


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. 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. 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.
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. 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. 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. 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.

Physical form

Contains lactose, potassium phosphate and citrate buffer salts, and mercaptosuccinic acid.

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

One unit will oxidize 1.0 μmole of acetaldehyde to acetic acid per min at 25 °C at pH 8.0 in the presence of β-NAD+, potassium and thiols.

Compare Similar Items

View Full Comparison

Show Differences

1 of 1

This Item
G6378G4134G3664
description

lyophilized powder, ≥2.0 units/mg protein

description

Type XV, lyophilized powder, 200-400 units/mg protein (modified Warburg-Christian)

description

Type IX, lyophilized powder, 200-400 units/mg protein (modified Warburg-Christian)

description

ammonium sulfate suspension, 100-300 units/mg protein (biuret)

specific activity

≥2.0 units/mg protein

specific activity

200-400 units/mg protein (modified Warburg-Christian)

specific activity

200-400 units/mg protein (modified Warburg-Christian)

specific activity

100-300 units/mg protein (biuret)

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

form

ammonium sulfate suspension

mol wt

228 kDa

mol wt

128 kDa

mol wt

128 kDa

mol wt

118 kDa

shipped in

dry ice

shipped in

dry ice

shipped in

dry ice

shipped in

-

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

2-8°C

Quality Level

200

Quality Level

300

Quality Level

200

Quality Level

200


Storage Class

11 - Combustible Solids

WGK

WGK 3

Flash Point (°F)

Not applicable

Flash Point (°C)

Not applicable

PPE (personal protective equipment)

Eyeshields, Gloves, type N95 (US)



Choose from one of the most recent versions:

Certificates of Analysis (COA)

Lot/Batch Number

It looks like we've run into a problem, but you can still download Certificates of Analysis from our Documents section.

If you need assistance, please contact Customer Support

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library




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).

      Helpful?

Reviews

No rating value

Active Filters