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P4234

Pyranose Oxidase from Coriolus sp.

recombinant, expressed in E. coli, ≥2.7 units/mg solid

Synonim(y):

Pyranose: Oxygen 2-Oxidoreductase

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Do Państwa/SKUDostępnośćCena netto
250 units
Skontaktuj się z Obsługą Klienta, aby uzyskać informacje na temat dostępności
1470,00 zł
1000 units
Skontaktuj się z Obsługą Klienta, aby uzyskać informacje na temat dostępności
5200,00 zł

Informacje o tej pozycji

Numer CAS:
UNSPSC Code:
12352204
NACRES:
NA.54
MDL number:
Specific activity:
≥2.7 units/mg solid
Recombinant:
expressed in E. coli

1470,00 zł


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recombinant

expressed in E. coli

Quality Segment

form

powder

specific activity

≥2.7 units/mg solid

shipped in

wet ice

storage temp.

−20°C

General description

Pyranose oxidase (P2O), a homotetrameric protein consists of a covalently bound flavin adenine dinucleotide (FAD). It is seen mostly among wood-degrading basidiomycetes.

Application

Pyranose Oxidase from Coriolus sp. has been used in the enzymatic oxidation of D-glucose (DG). It has also been used as a component in oxygen scavenging system (OSS) to increase the lifetime of the fluorophores.

Biochem/physiol Actions

Pyranose oxidase (P2O) can be used in clinical chemistry to determine 1,5-anhydro-d-glucitol marker, used for glycemic control in diabetes patients.
Pyranose oxidase (P2O) catalyzes the oxidation of aldopyranoses at position C-2 to yield the corresponding 2-ketoaldoses. The in vivo substrates of P2O are thought to be D-glucose, D-galactose, and D-xylose. They are oxidized to 2-keto-D-glucose (D-arabino-hexos-2-ulose, 2-dehydro-D-glucose), 2-keto-D-galactose (D-lyxo-hexos-2-ulose, 2-dehydro-D-galactose), and 2-keto-D-xylose (D-threopentos-2-ulose, 2-dehydro-D-xylose), respectively. Pyranose oxidase has significant activity with carbohydrates such as, L-sorbose, D-glucono-1,5-lactone, and D-allose. When pyranose oxidase catalyzes the oxidation of aldopyranoses, electrons are transferred to molecular oxygen which results in the formation of hydrogen peroxide[1].

Other Notes

Contains glutamate
One unit produces 1.0 μmol of hydrogen peroxide per minute at 37 °C, pH 7.0.
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Ta pozycja
P4105SAE0051G9637
description

recombinant, expressed in E. coli, ≥2.7 units/mg solid

description

lyophilized powder, ≥35 units/mg protein (biuret)

description

recombinant, expressed in E. coli, lyophilized powder

description

lyophilized powder, 40-80 units/mg solid, pH 8.1

specific activity

≥2.7 units/mg solid

specific activity

≥35 units/mg protein (biuret)

specific activity

≥35 unit/mg solid

specific activity

40-80 units/mg solid, pH 8.1

form

powder

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

recombinant

expressed in E. coli

recombinant

-

recombinant

expressed in E. coli

recombinant

-

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

2-8°C

shipped in

wet ice

shipped in

-

shipped in

-

shipped in

-

Quality Level

200

Quality Level

200

Quality Level

200

Quality Level

200


pictograms

Health hazard

signalword

Danger

hcodes

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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Questions

1–2 of 2 Questions  
  1. What is the solution stability for product P4234 after dilution?

    1 answer
    1. Prepare stock solutions in 0.1 M Tris-HCl, pH 7.0. While no specific concentration was provided, calculations based on the assay procedure suggest that stock solutions should be in the range of 0.5 - 1.0 mg/ml protein. This aligns with the general recommendation for proteins of a minimum of 1 mg protein/ml. The stock solution can be stored as aliquots at -20°C and should be reasonably stable for several months.

      Helpful?

  2. Do you have a protocol for the activity assay used to qualify pyranose oxidase?

    Do you have a protocol for the activity assay used to qualify pyranose oxidase?

    1 answer
    1. We do not have a pre-formulated protocol available at the moment. However, for reference, you may find the following publication informative. The publication, "Limited proteolysis of pyranose 2-oxidase results in a stable and active complex" in PeerJ Materials Science 2:e7 (https://doi.org/10.7717/peerj-matsci.7), served as the basis for this assay, utilizing the production of quinoneimine dye to directly reflect the turnover rate of pyranose oxidase.

      Helpful?

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