Accéder au contenu
Merck

C3515

Catalase from Aspergillus niger

ammonium sulfate suspension, ≥4,000 units/mg protein

Synonyme(s) :

H2O2:H2O2 oxidoreductase

Se connecter pour consulter les tarifs organisationnels et contractuels.

Sélectionner une taille de conditionnement

Changer de vue

A propos de cet article

Numéro CAS:
UNSPSC Code:
12352204
eCl@ss:
32160410
NACRES:
NA.54
Numéro CE :
MDL number:
Specific activity:
≥4,000 units/mg protein
Biological source:
Aspergillus niger
Service technique
Besoin d'aide ? Notre équipe de scientifiques expérimentés est là pour vous.
Laissez-nous vous aider


biological source

Aspergillus niger

Quality Segment

form

ammonium sulfate suspension

specific activity

≥4,000 units/mg protein

mol wt

tetramer ~250 kDa

storage condition

(Tightly closed)

technique(s)

FISH: suitable

UniProt accession no.

shipped in

wet ice

storage temp.

2-8°C

SMILES string

O(CC)C(=O)c1ccc(cc1)O

InChI

1S/C9H10O3/c1-2-12-9(11)7-3-5-8(10)6-4-7/h3-6,10H,2H2,1H3

InChI key

NUVBSKCKDOMJSU-UHFFFAOYSA-N

General description

Research area: Cell Signaling

Catalase is an active enzyme present in aerobic organisms. It is a ferric hemoprotein and a tetramer.

Application

Catalase from Aspergillus niger has been used:
  • as a positive control during the functional characterization of Clostridium difficile spore coat proteins.
  • as a component of the catalase solution to prepare GLOX buffer with enzymes to maintain the embryos of Caenorhabditis elegans before single-molecule fluorescence in situ hybridization (smFISH) studies
  • as a component of the imaging buffer for stochastic optical reconstruction microscopy (STORM) imaging of platelet-rich plasma
  • as a supplement in Todd Hewitt media plus 0.5 % yeast extract (THY) media for the neutralization of pneumococcal H2O2

Biochem/physiol Actions

Catalase catalyzes the decomposition of hydrogen peroxide into water and oxygen. Each subunit of the tetramer contains iron bound to a protoheme IX group. The enzyme also strongly binds NADP, which is in close proximity to the heme group. Isoelectric point is found to be 6.5. Optimum pH for catalytic activity is 7.0. The enzyme activity is inhibited by 3-amino-1-H-1,2,4 triazole, cyanide, azide, hydroxylamine, cyanogen bromide, 2-mercaptoethanol, dithiothreitol, dianisidine, and nitrate. Incubation of catalase with ascorbate or ascorbate/Cu2+ results in degradation of the catalase molecule.
Catalase is involved in catalyzing the degradation of hydrogen peroxide (H2O2) to water and free oxygen. Catalase is used commercially for decomposing H2O2 as it is added as an antimicrobial agent in process streams. It also catalyzes the oxidation of electron donors like ethanol and phenols during lower concentrations of H2O2. Catalase shows antioxidant activity by protecting cells from higher levels of reactive oxygen species (ROS). Increased expression of catalase is observed in chronic lymphocytic leukemia, gastric cancer, glioma, and melanoma. Decreased levels of catalase are seen in acute myeloid leukemia, lung, pancreatic, prostate, and skin (non-melanoma) cancers. Hence catalase exhibits a dual role in cancer.

Physical form

Suspension in 3.2 M (NH4)2SO4 solution, pH 6.0

Analysis Note

Protein determined by biuret

Other Notes

One unit will decompose 1.0 μmole of H2O2 per min at pH 7.0 at 25 °C, while the H2O2 concentration falls from 10.3 to 9.2 mM, measured by the rate of decrease of A240.

Disclaimer

Freezing of solutions is not recommended.


Classe de stockage

12 - Non Combustible Liquids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable



Faites votre choix parmi les versions les plus récentes :

Certificats d'analyse (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.

Si vous avez besoin d'assistance, veuillez contacter Service Clients

Déjà en possession de ce produit ?

Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.

Consulter la Bibliothèque de documents