Purified by affinity chromatography, Galanthus nivalis lectin (GNL/GNA) is composed of four identical subunits. GNL is a mannose-binding lectin, though [interestingly] it will not bind α-linked glucose. This lectin was one of the original molecules used to understand how proteins recognize carbohydrates. Galanthus nivalis is found to bind to many viral glycoproteins, making it a useful tool in HIV research studies.
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. Galanthus nivalis Lectin (GNL/GNA) is conjugated to HRP at an appropriate ratio to provide optimal staining characteristics.