GSL II is affinity purified tetramer that contains a single type of 30 kDa subunit. It has insecticidal structure/function, the first GlcNAc binding legume lectin proven to have insecticidal activity.
This lectin has a carbohydrate specificity for αGal and αGalNAc and elutes with galactose or N-acetylgalactosamine. Increasing the number of N-acetylglucosamine residues beyond two does not improve affinity. It has been reported to be unique in its ability to recognize exclusively α- or β-linked N-acetylglucosamine residues on the nonreducing terminal oligosaccharides. This lectin shows specificity for blood group A(-SA) greater than blood group B(-SA).
Alkaline phosphatase (AP) is conjugated to Griffonia simplicifolia Lectin (GSL II) to show the binding of GSL II 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.