Jacalin lectin (AIA) is purified by affinity chromatography and is tetrameric two-chain structure consisting of four identical protomers with an isoelectric point of pH 7.8. The lectin has specificity for blood group types O (+SA) and T. Jacalin is considered a galactose-specific lectin and elutes with galactose or melibiose. A post-translational proteolytic modification of Jacalin gives the lectin a novel carbohydrate-binding site involving the N terminus of the α-chain. The protein’s structure explains it’s carbohydrate-binding specificity of T-antigen disaccharide Galβ1,3GalNAc. Potent inhibitors of jacalin include D-galactose, β-Met-Gal and 2-deoxy-α-D-galactose.
Cy3 can be used to viualize the binding pattern of Artocarpus integrifolia (Jacalin) Lectin (AIA) in cellular imaging and flow cytometry. Cy3 is more photostable than many other flourophores and can be seen with TRITC filter sets. It is commonly combined with green-fluorescent dyes for dual-labeling.