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Merck

C1345

Sigma-Aldrich

Catalase from bovine liver

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

Sinónimos:

H2O2:H2O2 oxidoreductase

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About This Item

Número de CAS:
Comisión internacional de enzimas:
Número CE:
Número MDL:
Código UNSPSC:
12352204
eCl@ss:
32160410
NACRES:
NA.75

origen biológico

bovine liver

Nivel de calidad

Línea del producto

BioReagent

Formulario

powder

actividad específica

2,000-5,000 units/mg protein

mol peso

tetramer ~250 kDa

técnicas

cell culture | mammalian: suitable

punto isoeléctrico

5.4

Nº de acceso UniProt

Condiciones de envío

wet ice

temp. de almacenamiento

−20°C

cadena SMILES

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

Clave InChI

NUVBSKCKDOMJSU-UHFFFAOYSA-N

Información sobre el gen

cow ... CAT(280743)

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Descripción general

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.

Aplicación

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

Acciones bioquímicas o fisiológicas

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.

Precaución

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

Definición de unidad

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.

Nota de preparación

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.

Inhibidor

Referencia del producto
Descripción
Precios

Pictogramas

Health hazard

Palabra de señalización

Danger

Frases de peligro

Consejos de prudencia

Clasificaciones de peligro

Resp. Sens. 1

Código de clase de almacenamiento

11 - Combustible Solids

Clase de riesgo para el agua (WGK)

WGK 1

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable

Equipo de protección personal

Eyeshields, Gloves, type N95 (US)


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Visite la Librería de documentos

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
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
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

Protocolos

This procedure may be used for all Catalase products.

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