Catalog # or name ...
Purified from horseradish
The enzyme horseradish peroxidase (HRP), found in horseradish, is used extensively in molecular biology applications primarily for its ability to amplify a weak signal and increase detectability of a target molecule. HRP is often used in conjugates (molecules that have been joined genetically or chemically) to determine the presence of a molecular target. For example, an antibody conjugated to HRP may be used to detect a small amount of a specific protein in a western blot. Here, the antibody provides the specificity to locate the protein of interest and the HRP enzyme, in the presence of a substrate, produces a detectable signal. Horseradish peroxidase is also commonly used in techniques such as ELISA and Immunohistochemistry.
Peroxidase produced in horseradish has a molecular mass of 40 kDa.
myeloperoxidase; lactoperoxidase; verdoperoxidase; guaiacol peroxidase; thiocyanate peroxidase; eosinophil peroxidase; Japanese radish peroxidase; horseradish peroxidase (HRP); extensin peroxidase; heme peroxidase; MPO; oxyperoxidase; protoheme peroxidase; pyrocatechol peroxidase; scopoletin peroxidase; donor:hydrogen-peroxide oxidoreductase
Reddish-brown amorphous powder, lyophilized
Stable at -20℃ for at least one year
donor + H2O2 = oxidized donor + 2 H2O
< 50℃ (pH6.0,15min)
Cyanide, sulfide, fluoride, azide
≥250 Purpurogallin U/mg solid
One purpurogallin unit causes the formation of one milligram of purpurogallin in 20s at pH 6.0 at 20 °C.
The enzyme is reconstituted in 100mM phosphate buffer, pH 6.0 for activity assay.
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