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.
Alkaline phosphatase (AP) is conjugated to Galanthus nivalis Lectin (GNL/GNA) to show the binding of GNL/GNA in many applications including Western blotting and ELISA. Alkaline phosphatase is a large protein (140 kDa) that catalyzes the hydrolysis of phosphate groups from a substrate resulting in a colored or fluorescent product. The optimal enzymatic activity of this protein is between pH 8 and 10, and its reaction rate remains linear, improving sensitivity over time.