Horseradish Peroxidase (HRP)

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[ Source ] Armoracia rusticana
[ Appearance ] Red Brown Powder
[ Enzyme activity ] 100000u/g

[ Applications ]
1. RZ > 3, Activity > 250 U/mg: Primarily used in immunology; a high-purity peroxidase. Purified using specialized chromatographic techniques to remove Isoenzyme B, which can interfere with immunological reactions.
2. RZ > 2, Activity > 180 U/mg: Primarily used in clinical chemistry, as well as in immunological research.
3. RZ > 1, Activity > 100 U/mg: Primarily used in glucose test strips and urine analysis test strips.
4. RZ > 0.6, Activity > 60 U/mg: Primarily used in urine analysis test strips.

About Horseradish Peroxidase (HRP)
Horseradish Peroxidase (HRP) is a redox enzyme extracted from the roots of Armoracia rusticana and belongs to the peroxidase family. It functions by catalyzing the decomposition of hydrogen peroxide (H₂O₂) to generate reactive oxygen species, thereby oxidizing specific substrates (such as chromogenic agents or luminescent substances); consequently, it is widely utilized in biochemical assays, immunoassays, and molecular biology experiments.
Horseradish peroxidase is a commonly used enzyme in clinical diagnostic reagents. This product is not only extensively employed across various biochemical detection assays but is also widely incorporated into immunoassay kits, such as ELISA kits.
HRP is highly favored due to its inherent stability, abundant natural sources, and relatively low molecular weight, which facilitates the extraction of highly active, purified enzymes at a low cost. Furthermore, it exhibits excellent thermal stability and high substrate specificity; when conjugated to antigens or antibodies, it incurs minimal loss of enzymatic activity. The resulting enzyme-labeled antibodies retain both their functional binding sites and catalytic capabilities; moreover, HRP-labeled antibodies can maintain their full activity for a storage period of 1 to 2 years. Consequently, HRP currently stands as the most widely adopted and frequently used enzyme for labeling applications.
The application of horseradish peroxidase in the field of chemiluminescence is extensive, largely owing to its ability to catalyze chemiluminescent substrates to generate intense light signals. HRP catalyzes the oxidation of substrates—such as ABTS and TMB—into oxidized compounds that emit strong light signals within the visible spectrum. This characteristic endows HRP with significant advantages in fields such as chemiluminescent immunoassays, bioimaging, and DNA detection.
In chemiluminescent immunoassays, Horseradish Peroxidase is typically conjugated to antigens or antibodies to form a labeled complex. Once this labeled complex binds to the target antigen or antibody under investigation, the addition of appropriate substrates and oxidizing agents triggers HRP to catalyze the luminescence of the substrate, thereby enabling the detection and quantitative analysis of the target molecule. This methodology offers numerous advantages—including high sensitivity, high specificity, and operational simplicity—and is widely applied in clinical diagnostics, environmental monitoring, and food safety.
In the realm of bioimaging, Horseradish Peroxidase can be used to label specific biomolecules, such as proteins, antibodies, or nucleic acids. By employing chemiluminescence techniques, these labeled molecules can be visualized, thereby revealing their distribution and functional roles within biological systems. This method holds broad prospects for application in fields such as cell biology, molecular biology, and histology.
In addition to serving as a labeling enzyme, Horseradish Peroxidase can be utilized in immunoassays and chemiluminescence, the proteolytic inactivation of nucleases, the isolation of N-linked glycans, the performance validation of portable oxidative stress sensors, wastewater treatment, and food additives, among other applications.