Allium sativum lectin (ASA) is purified first with affinity chromatography and then with gel filtration. It is a dimer of two subunits. ASA binds to a number of Î±1-2-linked mannose residues. The lectin recognizes internal mannose and binds to the core pentasaccharide of N-linked glycans. In addition, the removal of sialic acids enhances binding activity. Horseradish peroxidase (HRP) is a 40 kDa protein that catalyzes the oxidation of substrates by hydrogen peroxide, resulting in a colored or fluorescent product or release of light as a byproduct of the reaction. It is most commonly used for blotting, immunoassays and immunohistochemistry methods. Allium sativum Lectin (ASA) is conjugated to HRP at an appropriate ratio to provide optimal staining characteristics.