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C1345

Sigma-Aldrich

Catalase from bovine liver

powder, suitable for cell culture, 2,000-5,000 units/mg protein

Synonyme(s) :

H2O2:H2O2 oxidoreductase

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About This Item

Numéro CAS:
Numéro de classification (Commission des enzymes):
Numéro CE :
Numéro MDL:
Code UNSPSC :
12352204
eCl@ss :
32160410
Nomenclature NACRES :
NA.75

Source biologique

bovine liver

Gamme de produits

BioReagent

Forme

powder

Activité spécifique

2,000-5,000 units/mg protein

Poids mol.

tetramer ~250 kDa

Technique(s)

cell culture | mammalian: suitable

Point isoélectrique

5.4

Numéro d'accès UniProt

Conditions d'expédition

wet ice

Température de stockage

−20°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

Informations sur le gène

cow ... CAT(280743)

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Description générale

CAT (catalase) is an endogenous antioxidant enzyme, thus conferring protection to cells against damage by ROS (reactive oxygen species). In humans, this gene is localized to chromosome 11p13, which is composed of 12 introns and 13 exons.
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.

Application

Catalase from bovine liver is used for the following applications:
  • Gel filtration
  • Analytical filtration on Ultrogel and glycerol gradient centrifugation
  • Size exclusion chromatography (HPLC)-HPLC analysis of estrogen receptor
  • Enzyme assays
  • Alcohol oxidase activity
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

Actions biochimiques/physiologiques

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.
This product doesn not need any activators, but it is inhibited by 3-amino-1-H-1,2,4 triazole, cyanide, azide, hydroxylamine, cyanogens bromide, 2-mercaptoethanol, dithiothreitol, dianisidnie and nitrate.

Attention

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

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 conc. falls from 10.3 to 9.2 mM, measured by the rate of decrease of A240.

Notes préparatoires

This product is a powder suitable for cell culture with activity at 2,000-5,000 units/mg. The enzyme is soluble in 50 mM potassium phosphate buffer at 1 mg/mL and pH 7.0.

Inhibiteur

Réf. du produit
Description
Tarif

Pictogrammes

Health hazard

Mention d'avertissement

Danger

Mentions de danger

Conseils de prudence

Classification des risques

Resp. Sens. 1

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

Claire M Doskey et al.
Redox biology, 10, 274-284 (2016-11-12)
Ascorbate (AscH-) functions as a versatile reducing agent. At pharmacological doses (P-AscH-; [plasma AscH-] ≥≈20mM), achievable through intravenous delivery, oxidation of P-AscH- can produce a high flux of H2O2 in tumors. Catalase is the major enzyme for detoxifying high concentrations
Theppanya Charoenrat et al.
Bioprocess and biosystems engineering, 27(6), 399-406 (2005-08-05)
An oxygen-limited fed-batch technique (OLFB) was compared to traditional methanol-limited fed-batch technique (MLFB) for the production of recombinant Thai Rosewood beta-glucosidase with Pichia pastoris. The degree of energy limitation, expressed as the relative rate of respiration (q(O)/q(O,max)), was kept similar
Yanqiong Liu et al.
Medicine, 94(13), e702-e702 (2015-04-04)
Reactive oxygen species (ROS) play critical roles in hepatocarcinogenesis. The catalase (CAT) enzyme is involved in the repair of ROS. Therefore, we investigate the association between CAT gene polymorphisms and the risk of hepatocellular carcinoma (HCC). A total of 715
G Redeuilh et al.
The Journal of biological chemistry, 262(15), 6969-6975 (1987-05-25)
The structure of the calf uterus nontransformed molybdate-stabilized estradiol receptor (ER) has been investigated using affinity labeling with tamoxifen aziridine and several monoclonal antibodies directed either against the steroid binding protein (Mr approximately 65,000) or against the heat shock protein
Taku Amo et al.
Journal of bacteriology, 184(12), 3305-3312 (2002-05-25)
We had previously isolated a facultatively anaerobic hyperthermophilic archaeon, Pyrobaculum calidifontis strain VA1. Here, we found that strain VA1, when grown under aerobic conditions, harbors high catalase activity. The catalase was purified 91-fold from crude extracts and displayed a specific

Protocoles

This procedure may be used for all Catalase products.

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