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E3289

Sigma-Aldrich

Catalase from bovine liver

≥20000 units/mg protein, lyophilized powder

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Synonym(s):
H2O2:H2O2 oxidoreductase
CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
NACRES:
NA.54

form

lyophilized powder

Quality Level

specific activity

≥20000 units/mg protein

mol wt

tetramer ~250 kDa

composition

protein, ≥60% E405

isoelectric point

5.4

shipped in

wet ice

storage temp.

−20°C

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

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This Item
C9322C1345C30
vibrant-m

E3289

Catalase from bovine liver

vibrant-m

C9322

Catalase from bovine liver

vibrant-m

C1345

Catalase from bovine liver

vibrant-m

C30

Catalase from bovine liver

form

lyophilized powder

form

lyophilized powder

form

powder

form

aqueous suspension

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

2-8°C

Quality Level

200

Quality Level

400

Quality Level

200

Quality Level

200

shipped in

wet ice

shipped in

wet ice

shipped in

wet ice

shipped in

wet ice

mol wt

tetramer ~250 kDa

mol wt

tetramer ~250 kDa

mol wt

tetramer ~250 kDa

mol wt

tetramer ~250 kDa

General description

Catalase is encoded by the gene mapped to human chromosome 11p13. Mammalian catalase is an antioxidant enzyme and is a member of hydroperoxidase family). The active enzyme is homotetrameric in nature.

Application

Catalase from bovine liver has been used as a component of gloxy, which is one of the most popular oxygen-scavenging systems.
Catalase acts as a natural antioxidant to study the roles of reactive oxygen species in gene expression and apoptosis. It has also been used to protect against oxidative damage to proteins, lipids, and nucleic acids. Industrially, catalses have been used to remove hydrogen peroxide added to milk and cheese, in textile bleaching, and to examine its positive effects on the viability of DNA-repair mutants of E. coli.

Biochem/physiol Actions

Catalase has an ability to convert solar radiation into reactive oxidant species (ROS). It is involved in regulation of tissue peroxide levels. Mutation in catalase gene result in the progress of essential hypertension (EH).
Catalase catalyzes the degradation of hydrogen peroxide into water and oxygen. It can also react with alkylhydrogen peroxides, such as methylperoxide and ethylperoxide and the second H2O2 molecule can be replaced by methanol, ethanol, propanol, formate and nitrate as a hydrogen donor.

Components

Catalase from bovine liver is a tetramer consisting of 4 equal subunits each with a 60 kDa molecular weight. Each of these subunits contains iron bound to a protoheme IX group. The enzyme will also strongly bind to NADP, where NADP and the heme group are within 13.7 angstroms.

Unit Definition

One unit will decompose 1.0 micromole of hydrogen peroxide per minute at pH 7.0 at 25 deg C, while the hydrogen peroxide concentration falls from 10.3 to 9.2 millimolar.

Physical form

Supplied as a lyophilized powder containing ≤0.2% thymol

pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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Influence of A-21T and C-262T genetic polymorphisms at the promoter region of the catalase (CAT) on gene expression.
Saify K, et al.
Environmental Health and Preventive Medicine, 21(5), 382-386 (2016)
Mechanisms of oxidant generation by catalase.
Heck D E, et al.
Annals of the New York Academy of Sciences, 1203(1), 120-125 (2010)
Frequent loss of heterozygosity on chromosomes 3p and 17p without VHL or p53 mutations suggests involvement of unidentified tumor suppressor genes in follicular thyroid carcinoma.
Grebe S K, et al.
The Journal of Clinical Endocrinology and Metabolism, 82(11), 3684-3691 (1997)
Observation and Analysis of RAD51 Nucleation Dynamics at Single-Monomer Resolution.
Subramanyam S, et al.
Methods in Enzymology, 600, 201-232 (2018)
Jiawei Sun et al.
ACS nano, 13(9), 10191-10200 (2019-08-28)
Self-propelled motors have been developed with promising potential for medical applications. However, most of them have a size range at the microscale, which limits their further research for in vivo experiments. Previously, our group developed nanoscaled motors with a size

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