Horseradish Peroxidase Activators

Horseradish Peroxidase Activators include a range of substrates and modifiers that enhance the enzyme's functionality in biochemical reactions and diagnostic assays. Key among these activators is Hydrogen Peroxide, which acts as a substrate enabling Horseradish Peroxidase's catalytic activity. This interaction is fundamental to the enzyme's function in oxidizing various organic and inorganic compounds. Phenol, 4-Aminoantipyrine, and o-Dianisidine serve as substrates that, in the presence of hydrogen peroxide, are oxidized by Horseradish Peroxidase to produce colored or fluorescent products. These reactions are crucial in various biochemical assays, including quantitative determinations in enzymatic tests.

Additionally, 3,3',5,5'-Tetramethylbenzidine (TMB) and ABTS undergo oxidation by Horseradish Peroxidase in the presence of hydrogen peroxide, resulting in color changes used to measure enzyme activity in assays like ELISA. Guaiacol and Amplex Red are also oxidized to colored or fluorescent products, expanding the range of assays where Horseradish Peroxidase activity is essential. Luminol's chemiluminescence upon oxidation by Horseradish Peroxidase underlies its use in forensic and biological research. Substrates like p-Cresol and ferrocyanide further demonstrate the enzyme's versatility in producing detectable products in various assay formats. N-Ethylmaleimide, though not a substrate, enhances Horseradish Peroxidase's stability, indirectly augmenting its activity across a spectrum of applications. Collectively, these activators highlight the multifaceted role of Horseradish Peroxidase in scientific and diagnostic fields, showcasing its pivotal function in catalyzing reactions that form the basis of numerous analytical techniques.