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C30
Catalase from bovine liver
aqueous suspension, 10,000-40,000 units/mg protein
Synonym(s):
Bovine hepatocatalase, H2O2:H2O2 oxidoreductase
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About This Item
CAS Number:
UNSPSC Code:
12352204
eCl@ss:
32160410
NACRES:
NA.54
MDL number:
Specific activity:
10,000-40,000 units/mg protein
Biological source:
bovine liver
Concentration:
20-50 mg/mL
Pricing and availability is not currently available.
biological source
bovine liver
Quality Level
form
aqueous suspension
specific activity
10,000-40,000 units/mg protein
mol wt
tetramer ~250 kDa
concentration
20-50 mg/mL
technique(s)
GC/MS: suitable
isoelectric point
5.4
UniProt accession no.
shipped in
wet ice
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This Item | |||
|---|---|---|---|
| technique(s) GC/MS: suitable | technique(s) - | technique(s) - | technique(s) - |
| biological source bovine liver | biological source - | biological source bovine liver | biological source - |
| specific activity 10,000-40,000 units/mg protein | specific activity 40,000-60,000 units/mg protein (E1%/405) | specific activity 2,000-5,000 units/mg protein | specific activity ≥10,000 units/mg protein |
| Gene Information cow ... CAT(280743) | Gene Information cow ... CAT(280743) | Gene Information cow ... CAT(280743) | Gene Information cow ... CAT(280743) |
| concentration 20-50 mg/mL | concentration - | concentration - | concentration - |
| form aqueous suspension | form aqueous suspension | form lyophilized powder | form lyophilized powder |
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.
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 contains 506 residues. It is a tetramer and each monomer corresponds to a molecular weight of 61 kDa. The active site in each momomer comprises nicotinamide adenine dinucleotide phosphate (NADPH) and iron binding region.
Research area: Cell Signaling
Research area: Cell Signaling
Application
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
Catalase from bovine liver is used for the following applications:
- Dielectrophoretic field-flow fractionation (DEP-FFF): It is a chromatographic method in which cell elution times reflect the positions of cells in a hydrodynamic flow profile under the control of sedimentation, DEP and hydrodynamic lift forces, FSED, FDEP and FHDL, respectively. The DEP-FFF buffer consists of catalase along with other ingrediants.[1][2]
- GC-MS analyses.[3]
- Deionization.[4]
- GC-FID analysis.5
- Functional analysis of blood vessel.[5]
Catalase from bovine liver has been used for measuring the hydrogen peroxide content in cancer tissue homogenates. It has also been used to test the effect of organophosphate insecticide chlorpyrifos-ethyl (CE) [0,0-diethyl 0 (3,5,6-trichloro-2-pyridyl) phosphorothioate] on its enzyme activity.
Biochem/physiol Actions
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′t 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.
Preparation Note
This product is a crystalline suspension in water containing 0.1% thymol with activity of 10,000-40,000 units/mg.
Tightly closed. Dry. Keep locked up or in an area accessible only to qualified or authorized
persons
persons
Other Notes
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.
Disclaimer
Solutions of catalse should not be frozen. Frozen solution will result in a 50-70% loss of activity.
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Product No.
Description
Pricing
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
13 - Non Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US), type N95 (US)
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The effect of organophosphate insecticide chlorpyrifos-ethyl on lipid peroxidation and antioxidant enzymes (in vitro)
Gultekin F, et al.
Archives of Toxicology, 74(9), 533-538 (2000)
The complete amino acid sequence of bovine liver catalase and the partial sequence of bovine erythrocyte catalase
Schroeder WA, et al.
Archives of Biochemistry and Biophysics, 214(1), 397-421 (1982)
Haïfa Debbabi et al.
Molecules (Basel, Switzerland), 25(9) (2020-05-07)
The present investigation was focused on the study of the chemical composition variability and biological activities of the essential oils from Clinopodium nepeta subsp. nepeta and subsp. glandulosum. Essential oils extraction was performed using hydrodistillation and the separation of the
Sixty years from discovery to solution: crystal structure of bovine liver catalase form III
Foroughi LM, et al.
Acta Crystallographica Section D, Biological Crystallography, 67(9), 756-762 (2011)
Stéphanie Heuskin et al.
Journal of chromatography. A, 1216(14), 2768-2775 (2008-10-28)
The chemical composition of Matricaria chamomilla L. and Nepeta cataria L. essential oils was determined by GC-MS on an apolar stationary phase by comparison of the characteristic fragmentation patterns with those of the Wiley 275L database. The GC-MS chromatograms were
Related Content
Product Information Sheet
Global Trade Item Number
| SKU | GTIN |
|---|---|
| 49451-U | 04061837619304 |
| 577141-U | 04065269130505 |
| 577140-U | 04065265824255 |
| C30-1G | 04061826303849 |
| C30-100MG | 04061833484982 |
| C30-500MG | 04061833484999 |
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