Peroxidase from horseradish - HRP

Horseradish peroxidase (HRP) is isolated from horseradish roots (Amoracia rusticana) and belongs to the ferroprotoporphyrin group of peroxidases. The catalytic reaction of Horseradish peroxidase is used to amplify a weak signal and increase detectability of a target molecule, such as a protein. When incubated with a substrate, horseradish peroxidase produces a coloured (fluorimetric, or luminescent) derivative of the labeled molecule, allowing quantification. For this HRP is widely used in biochemistry applications such as western blots, ELISA and Immunohistochemistry. 

Our product is an essentially salt free lyophilized powder that can be used to determine amounts of glucose and peroxides in solution.

Biochemical Features:
- HRP readily combines with hydrogen peroxide (H2O2) and the resulting complex can oxidize a wide variety of hydrogen donors.
- The optimal pH is 6.0-6.5 and the enzyme is most stable in the pH range of 5.0-9.0.
- HRP can be conjugated to antibodies by several different methods including glutaraldehyde, periodate oxidation, through disulfide bonds, and also via amino and thiol directed cross-linkers.
- HRP is smaller and more stable than β-galactosidase or alkaline phosphatase and therefore, HRP is the more desired label. 

Known inhibitors are sodium azide, cyanide, L-cystine, dichromate, ethylenethiourea, hydroxylamine, sulfide, vanadate, p-aminobenzoic acid, and Cd2+, Co2+, Cu2+, Fe3+, Mn2+, Ni2+, and Pb2+ ions.