Peroxidase from horseradish

Horseradish peroxidase (HRP) is isolated from horseradish roots (Amoracia rusticana). HRP is a single chain polypeptide containing four disulfide bonds. Its molecular weight (~44 kDa) includes the polypeptide chain (33,890 Daltons), hemin plus Ca2+ (~700 Daltons), and carbohydrate (~9,400 Daltons). At least seven isozymes of HRP exist. The isoelectric point for horseradish peroxidase isozymes is 3.0 - 9.0.

Horseradish peroxidase is isolated from horseradish roots (Amoracia rusticana) and belongs to the ferroprotoporphyrin group of peroxidases. HRP is a single chain polypeptide containing four disulfide bridges. It is a glycoprotein containing 18% carbohydrate. The carbohydrate composition consists of galactose, arabinose, xylose, fucose, mannose, mannosamine, and galactosamine depending upon the specific isozyme. Its molecular weight (~44 kDa) includes the polypeptide chain (33,890 Daltons), hemin plus Ca²⁺ (~700 Daltons), and carbohydrate (~9,400 Daltons). At least seven isozymes of HRP exist. The isoelectric point for horseradish peroxidase isozymes ranges from 3.0 - 9.0.

HRP is used in immunoassays, such as ELISAs, Western blots, and lateral flow assays. HRP is used in academic research, diagnostics, and pharmaceutical research. For more applications, see the following technical article: An Introduction to Horseradish Peroxidase (HRP) and Its Applications.

Peroxidase from horseradish has been used in western blotting.

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The RZ (Reinheitszahl) is the absorbance ratio A₄₀₃/A₂₇₅ determined at 0.5-1.0 mg/ml in deionized water. It is a measure of hemin content, not enzymatic activity. Even preparations with high RZ may have low enzymatic activity.

One pyrogallol unit will form 1.0 mg purpurogallin from pyrogallol in 20 sec at pH 6.0 at 20 °C.

View more information on peroxidase at www.sigma-aldrich.com/enzymeexplorer.

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