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C3155

Sigma-Aldrich

Catalase from bovine liver

aqueous solution, ≥30,000 units/mg protein

Sinonimo/i:

H2O2:H2O2 oxidoreductase

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About This Item

Numero CAS:
Classificazione EC (Enzyme Commission):
Numero MDL:
Codice UNSPSC:
12352200
NACRES:
NA.32

Origine biologica

bovine liver

Livello qualitativo

Descrizione

optimum pH ~ 7.0

Sterilità

aseptically filled

Forma fisica

aqueous solution

Attività specifica

≥30,000 units/mg protein

PM

tetramer ~250 kDa

contiene

≤0.10 mg/mL Thymol

Composizione

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

Condizioni di stoccaggio

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

tecniche

activity assay: suitable

Punto isoelettrico

5.4

pI 

5.4

N° accesso UniProt

Condizioni di spedizione

wet ice

Temperatura di conservazione

2-8°C

InChI

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

Informazioni sul gene

cow ... CAT(280743)

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Descrizione generale

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.

Applicazioni

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

Azioni biochim/fisiol

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.

Avvertenza

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

Definizione di unità

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.

Nota sulla preparazione

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.

Inibitore

N° Catalogo
Descrizione
Determinazione del prezzo

Pittogrammi

Health hazard

Avvertenze

Danger

Indicazioni di pericolo

Consigli di prudenza

Classi di pericolo

Resp. Sens. 1

Codice della classe di stoccaggio

12 - Non Combustible Liquids

Classe di pericolosità dell'acqua (WGK)

WGK 1

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable

Dispositivi di protezione individuale

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


Certificati d'analisi (COA)

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Camilla Ciolli Mattioli et al.
Nucleic acids research, 47(5), 2560-2573 (2018-12-28)
The proper subcellular localization of RNAs and local translational regulation is crucial in highly compartmentalized cells, such as neurons. RNA localization is mediated by specific cis-regulatory elements usually found in mRNA 3'UTRs. Therefore, processes that generate alternative 3'UTRs-alternative splicing and
Trine Juul et al.
The Journal of biological chemistry, 285(28), 21411-21415 (2010-05-11)
Hydroxyurea (HU) is a well tolerated ribonucleotide reductase inhibitor effective in HIV, sickle cell disease, and blood cancer therapy. Despite a positive initial response, however, most treated cancers eventually progress due to development of HU resistance. Although RNR properties influence
Investigation of the binding mechanism and inhibition of bovine liver catalase by quercetin: Multi-spectroscopic and computational study
Samaneh R, et al.
BioImpacts, 7(3), 147?153-147?153 (2017)
Koodathingal Prakash et al.
Protein science : a publication of the Protein Society, 11(1), 46-57 (2001-12-14)
Catalases, although synthesized from single genes and built up from only one type of subunit, exist in heterogeneous form with respect to their conformations and association states in biological systems. This heterogeneity is not of genetic origin, but rather reflects
Namrta Purwar et al.
Biochemistry, 50(21), 4491-4503 (2011-04-29)
We present the structures of bovine catalase in its native form and complexed with ammonia and nitric oxide, obtained by X-ray crystallography. Using the NO generator 1-(N,N-diethylamino)diazen-1-ium-1,2-diolate, we were able to generate sufficiently high NO concentrations within the catalase crystals

Protocolli

This procedure may be used for all Catalase products.

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