Horseradish Peroxidase Seller

Product name:Horseradish Peroxidase
Description of Horseradish Peroxidase:
Horseradish Peroxidase uses hydrogen peroxide to oxidize both organic and inorganic compounds.1 Horseradish peroxidase along with other heme peroxidases are brightly colored especially under the near-ultraviolet light.2 This property of heme peroxidases make them useful for attaching to “transparent” proteins so that they can be seen under different wavelengths. The heme group that is in horseradish peroxidase is simpler than those in mammalians and therefore makes it an excellent starting point in the in-depth study of heme peroxidases and their functions.2  It has been found that horseradish peroxidase when combined with other compounds is highly reactive toward human tumor cells.  A better understanding of horseradish peroxidase could lead to a new targeted cancer therapy.
Horseradish Peroxidase (HRP), a plant glycoprotein with a molecular weight of 40,000 D and a molecular radius (ae) of 30 A, has been modified chemically to prepare tracer molecules with different molecular charge. Modification of free carboxyl groups on the enzyme is achieved by carbodiimide activation and subsequent reaction of activated carboxyl groups with a nucleophile; uncharged groups or radicals containing additional positively charged moieties are introduced into the protein molecule resulting in an increased net positive charge of the tracer. Amino groups in the protein molecule are modified by acetylation or succinylation; this reaction will increase the net negative charge of the enzyme by either introducing an uncharged group or an additional carboxyl radical. The tracer molecules so obtained are then characterized in terms of molecular size and charge by column chromatography and isoelectric focusing respectively. The enzymatic activity as measured by 3,3'-diaminobenzidine reaction, the pH optimum and the absorption spectra for the modified enzymes remain virtually unchanged.
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