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A6941

Alcohol Oxidase from Candida boidinii

lyophilized powder, 5-15 units/mg protein

Sinónimos:

AOD1, AOX, Alcohol:oxygen oxidoreductase

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Tamaño de envaseSKUDisponibilidadPrecio
50 units
Comprobar disponibilidad del carrito
$467.00

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Número CAS:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-971-3
MDL number:
Número CE:
Specific activity:
5-15 units/mg protein
Biological source:
fungus (Candida boidinii)

$467.00


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biological source

fungus (Candida boidinii)

Quality Level

form

lyophilized powder

specific activity

5-15 units/mg protein

mol wt

octomer 600 kDa by sedimentation equilibrium

solubility

100 mM potassium phosphate, pH 7.5: soluble 1.0 mg/mL at 25 °C (Cold)

storage temp.

−20°C

General description

Research area: Cell Signaling

Alcohol Oxidase (AOX) is a homo-octamer composed of eight flavin adenine dinucleotide (FAD) cofactors and belongs to the glucose-methanol-choline (GMC) family of oxidoreductases. The AOX1 and AOX2 genes are responsible for encoding AOX.[1] Alcohol oxidase is primarily localized in the peroxisome but is also found in the cytoplasm.[2] Alcohol oxidase is a 600 kDa homooctomeric flavoprotein with eight equal 74 kDa subunits; each containing a flavin adenine dinucleotide (FAD) molecule.[3]

Application

Alcohol oxidase has been used:
  • to catalyze the oxidation of short-chain, primary, aliphatic alcohols to their respective aldehydes [2].
  • to study methanol metabolism in yeasts, such as Candida, Pichia, and Hansenula.
  • to study protein translocation into peroxisomes.
  • for the determination of ethanol concentration in alcoholic drinks using enzymatic assay.[4]
  • in development of enzyme electrode for the determination of alcohols.[5]

Biochem/physiol Actions

Alcohol oxidase has the highest affinity for methanol. The affinity decreases with increasing chain length of the alkyl (R) group. The enzyme shows little activity toward secondary, tertiary, or aromatic alcohols; or aliphatic alcohols with a chain length of more than 5 carbons. The pH range for activity of this product is 6.5-8.5, with the optimum pH being 7.5. Alcohol oxidases facilitate the conversion of alcohol into carbonyl compounds while producing hydrogen peroxide.[1] It is also the first enzyme in the yeast methanol utilization pathway.[1]

Physical form

Contains potassium phosphate buffer salts, DTE, and stabilizer

Other Notes

One unit will oxidize 1.0 μmole of methanol to formaldehyde per min at pH 7.5 at 25 °C.

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Este artículo
F8649G7400C1235
specific activity

5-15 units/mg protein

specific activity

5.0-15.0 units/mg protein

specific activity

≥3,000 units/g solid

specific activity

≥10 units/mg protein

biological source

fungus (Candida boidinii)

biological source

fungus (Candida boidinii)

biological source

fungus (Dactylium dendroides)

biological source

-

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

storage temp.

−20°C

storage temp.

2-8°C

storage temp.

−20°C

storage temp.

−20°C

mol wt

octomer 600 kDa by sedimentation equilibrium

mol wt

-

mol wt

-

mol wt

55 kDa

solubility

100 mM potassium phosphate, pH 7.5: soluble 1.0 mg/mL at 25 °C (Cold)

solubility

-

solubility

-

solubility

50 mM potassium phosphate buffer, pH 7.0: soluble


Clase de almacenamiento

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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Protocolos

To measure alcohol oxidase activity, this assay uses 2,2′-azino-bis-(3-ethylbenzothiazoline-6-sulfonic acid) and a continuous spectrophotometric rate determination at 405 nm.


H R Waterham et al.
The Journal of cell biology, 139(6), 1419-1431 (1998-02-12)
Alcohol oxidase (AOX), the first enzyme in the yeast methanol utilization pathway is a homooctameric peroxisomal matrix protein. In peroxisome biogenesis-defective (pex) mutants of the yeast Pichia pastoris, AOX fails to assemble into active octamers and instead forms inactive cytoplasmic
H Gülce et al.
Biosensors & bioelectronics, 17(6-7), 517-521 (2002-04-18)
A new enzyme electrode for the determination of alcohols was developed by immobilizing alcohol oxidase in polvinylferrocenium matrix coated on a Pt electrode surface. The amperometric response due to the electrooxidation of enzymatically generated H(2)O(2) was measured at a constant
B Vinet
Clinical chemistry, 33(12), 2204-2208 (1987-12-01)
This method for the specific determination of methanol in serum is based on the following two reactions: (formula; see text) Alcohol oxidase is not specific: it converts all lower alcohols to their corresponding aldehydes; however, formaldehyde dehydrogenase is specific and



Número de artículo de comercio global

SKUGTIN
A6941-250UN04061832727875
A6941-50UN04061832727882

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