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Merck
CN

C3515

Catalase from Aspergillus niger

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

Synonym(s):

H2O2:H2O2 oxidoreductase

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About This Item

CAS Number:
UNSPSC Code:
12352204
eCl@ss:
32160410
NACRES:
NA.54
EC Number:
MDL number:
Specific activity:
≥4,000 units/mg protein
Biological source:
Aspergillus niger
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biological source

Aspergillus niger

Quality Level

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.


Storage Class

12 - Non Combustible Liquids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

Regulatory Information

常规特殊物品

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Protocols

过氧化氢酶催化过氧化氢生成水和氧气。该实验方案使用分光光度法测定过氧化氢酶活性。

This procedure may be used for all Catalase products.

Articles

以硫酸铵悬浮液形式提供的酶的使用指南

Instructions for working with enzymes supplied as ammonium sulfate suspensions


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
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
M E Percy
Canadian journal of biochemistry and cell biology = Revue canadienne de biochimie et biologie cellulaire, 62(10), 1006-1014 (1984-10-01)
Although animal catalase has been studied for decades, its physiological role has remained perplexing. It has two enzymatic functions, not only catalyzing the breakdown of H2O2 into O2 and H2O, but also in the presence of low concentrations of H2O2



Global Trade Item Number

SKUGTIN
C3515-10MG04061833485941
C3515-100MG04061832729107
C3515-25MG04061833485958