Catalase from bovine liver is a homotetrameric enzyme that is primarily located in peroxisomes.
- Activates the decomposition of hydrogen peroxide
- Natural antioxidant used to study roles of reactive oxygen species
- Catalyzes the decomposition of hydrogen peroxide into water and oxygen
Catalase is a tetramer consisting of 4 equal subunits with a molecular weight of 60 kDa each. Each subunit contains iron bound to a protoheme IX group. The enzyme also strongly binds NADP, which is in close proximity to the heme group (13.7 Å apart). Catalase catalyzes the following reaction: 2 H2O2→O2 + 2 H2O Catalase can also react with alkylhydrogen peroxides instead of H2O2, such as methylperoxide and ethylperoxide. Catalase does not require any activator for exhibiting its catalytic activity. Catalase activity is constant over the pH range of 4.0-8.5.
Catalase is often used as an antioxidant in cell culture media. It has been used to study the role of ROSs in gene expression and apoptosis, mainly in cancer researches. Catalase is used to eliminate H2O2 from enzymatic oxidation reactions.
Specific Activity: ~30,000 u/mL ; ≥40,000 u/mg protein
Key Applications: Enzymes, Inhibitors, Substrates
Application Areas: Molecular Biology, Culture media
Product Type: Proteins, Enzymes & Peptides
Extinction Coefficient (E1%): 36.5 (276 nm)(Lit.)
Presentation: Clear, Pale Yellow Solution
Format: Sterile Aqueous Solution
Isoelectric point (pI): 5.4(Lit.)
NOTES: Stoke's radius: 5.12 nm -Catalase does not require any activators, but is inhibited by 3-amino-1-H-1,2,4 triazole, cyanide, azide, hydroxylamine, cyanogen bromide, 2-mercaptoethanol, dithiothreitol, dianisidine, and nitrate. Catalase is also inhibited by ascorbate and ascorbate with Cu2+. Incubation of catalase with ascorbate or ascorbate/Cu2+ results in degradation of the catalase molecule.
Solubility: Miscible in water.
Sterility: Sterile aqueous solution
Storage & Handling: Store at +4°C, do not freeze.