C3515
Catalase from Aspergillus niger
ammonium sulfate suspension, ≥4,000 units/mg protein
Synonyme(s) :
H2O2:H2O2 oxidoreductase
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About This Item
Numéro CAS:
Numéro MDL:
Code UNSPSC :
12352204
eCl@ss :
32160410
Nomenclature NACRES :
NA.54
Source biologique
Aspergillus niger
Forme
ammonium sulfate suspension
Activité spécifique
≥4,000 units/mg protein
Poids mol.
tetramer ~250 kDa
Conditions de stockage
(Tightly closed)
Technique(s)
FISH: suitable
Conditions d'expédition
wet ice
Température de stockage
2-8°C
InChI
1S/C9H10O3/c1-2-12-9(11)7-3-5-8(10)6-4-7/h3-6,10H,2H2,1H3
Clé InChI
NUVBSKCKDOMJSU-UHFFFAOYSA-N
Description générale
Research area: Cell Signaling
Catalase is an active enzyme present in aerobic organisms. It is a ferric hemoprotein and a tetramer.
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
Actions biochimiques/physiologiques
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.
Attention
Freezing of solutions is not recommended.
Définition de l'unité
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.
Forme physique
Suspension in 3.2 M (NH4)2SO4 solution, pH 6.0
Remarque sur l'analyse
Protein determined by biuret
Anticorps
Réf. du produit
Description
Tarif
Enzyme
Réf. du produit
Description
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Inhibiteur
Réf. du produit
Description
Tarif
Produit(s) apparenté(s)
Code de la classe de stockage
12 - Non Combustible Liquids
Classe de danger pour l'eau (WGK)
WGK 1
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Certificats d'analyse (COA)
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Les clients ont également consulté
Jacek Switala et al.
Archives of biochemistry and biophysics, 401(2), 145-154 (2002-06-11)
Catalases from 16 different organisms including representatives from all three phylogenetic clades were purified and characterized to provide a comparative picture of their respective properties. Collectively the enzymes presented a diverse range of activities and properties. Specific activities ranged from
Seleipiri Charles et al.
Analytical chemistry, 93(3), 1369-1376 (2020-12-24)
Recent development in fluorescence-based molecular tools has contributed significantly to developmental studies, including embryogenesis. Many of these tools rely on multiple steps of sample manipulation, so obtaining large sample sizes presents a major challenge as it can be labor-intensive and
3D structure modeling of catalase enzyme from Aspergillus Fumigatus
Dwivedi V D, et al.
Open journal of immunology, 1(1) (2016)
J Fiedurek et al.
Journal of applied microbiology, 89(1), 85-89 (2000-08-17)
A novel method for increasing dissolved oxygen concentration in culture media has been developed. It involves adding hydrogen peroxide (H2O2) to the medium which is then decomposed to oxygen and water by catalase. Some factors affecting oxygenation of culture were
L Brunelli et al.
Free radical biology & medicine, 30(7), 709-714 (2001-03-29)
Previously, we found that catalase enhanced the protection afforded by superoxide dismutase to Escherichia coli against the simultaneous generation of superoxide and nitric oxide (Brunelli et al., Arch. Biochem. Biophys. 316:327-334, 1995). Hydrogen peroxide itself was not toxic in this
Articles
Instructions for working with enzymes supplied as ammonium sulfate suspensions
Protocoles
This procedure may be used for all Catalase products.
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