E3289
Catalase from bovine liver
≥20000 units/mg protein, lyophilized powder
Synonym(s):
H2O2:H2O2 oxidoreductase
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About This Item
form
lyophilized powder
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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General description
Research area: Cell Signaling
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.
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.
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.
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 has been used:
- as a component of gloxy, which is one of the most popular oxygen-scavenging systems.
- in single molecule fluorescence resonance energy transfer (FRET) measurements.
- in cytochrome-C oxidase (COX) histochemistry to study the role of mitochondrial uncoupling protein 2 (UCP2) in limiting oxidative stress during glaucoma.
- to pre-treat slide chambers for total internal reflection fluorescence (TIRF) microscopy.
- in quantifying hydrogen peroxide release.
- to help minimize the effects of reactive oxygen species (ROS) in cooperativity assay for studying doublecortin and microtubule interaction.
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:
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 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, 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.
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
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
Storage Class Code
11 - Combustible Solids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
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’.
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