Skip to Content
MilliporeSigma
All Photos(1)

Documents

C3155

Sigma-Aldrich

Catalase from bovine liver

aqueous solution, ≥30,000 units/mg protein

Synonym(s):

H2O2:H2O2 oxidoreductase

Sign Into View Organizational & Contract Pricing


About This Item

CAS Number:
Enzyme Commission number:
MDL number:
UNSPSC Code:
12352200
NACRES:
NA.32

biological source

bovine liver

Quality Level

description

optimum pH ~ 7.0

sterility

aseptically filled

form

aqueous solution

specific activity

≥30,000 units/mg protein

mol wt

tetramer ~250 kDa

contains

≤0.10 mg/mL Thymol

composition

ammonium sulphate, 30-50%
catalase, 10-20%

storage condition

(Tightly closed. Keep locked up or in an area accessible only to qualified or authorized
persons)

technique(s)

activity assay: suitable

isoelectric point

5.4

pI 

5.4

UniProt accession no.

shipped in

wet ice

storage temp.

2-8°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

Gene Information

cow ... CAT(280743)

Looking for similar products? Visit Product Comparison Guide

General description

Research Area: Cell Signaling

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.
Research area: Cell Signaling

Catalase from bovine is a tetrameric enzyme, consisting of four identical sub-units containing a single heme moiety per subunit. Each subunit has four domains like the α-helical domain, an eight-stranded β-barrel, N-terminal threading arm that is connected to the β-barrel via a wrapping loop.

Application

Catalase from bovine liver has been used:

  • as a component of the GLOX buffer during single molecule fluorescent in situ hybridization (smFISH) on primary mouse cortical neurons
  • for its structural and kinetic analysis of its interaction with nitric oxide
  • in the preparation of glucose oxidase-catalase system (GOX-CAT system) to generate H2O2 and study the effect of H2O2-induced oxidative stress on myelination in mouse organotypic cerebellar slice cultures
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, catalzes 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.

Catalase from bovine liver may be used:

  • to prepare H2O2-O2 based biocathode for applications in glucose biofuel cells
  • to study the kinetic properties and storage stability of catalase immobilized on to florisil
  • in glutathione-mediated superoxide generation in an aqueous solution

Biochem/physiol Actions

Catalase is an active, ubiquitous enzyme that is found in all aerobic organisms. Lower levels of catalase and oxidative stress lead to several disorders such as vitiligo, hypertension, acatalasemia, cancer, diabetes mellitus, and Alzheimer’s.
Catalase, an antioxidant enzyme found in all aerobic organisms, catalyzes the degradation of hydrogen peroxide, a byproduct of metabolic processes, into less harmful 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. Catalase enzyme uses either iron (Fe) or manganese (Mn) as cofactor, and are classified as Fe-CAT or Mn-CAT.

Caution

Solutions of catalse should not be frozen. Frozen solution will result in a 50-70% loss of activity.

Unit Definition

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.

Preparation Note

This product is an aqueous solution containing >30,000 units/mg protein. To remove the thymol preservative, the catalase crystals may be pelleted by centrifugation, the supernatant, discarded, the pellet resuspended in water, and then pelleted again. The enzyme is soluble in 50 mM potassium phosphate buffer at 1 mg/mL and pH 7.0.

pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service