Griffonia (Bandeiraea) simplicifolia lectin II (GSL II, BSL II)

This lectin is a tetrameric glycoprotein composed of four subunits of nearly identical size. Each 30,000 dalton subunit has a binding site for alpha- or beta-linked N-acetylglucosamine residues. Unlike other N-acetylglucosamine specific lectins, increasing the number of N-acetylglucosamine residues beyond two does not improve affinity. GSL II has been reported to be unique in its ability to recognize exclusively alpha- or beta-linked N-acetylglucosamine residues on the nonreducing terminal of oligosaccharides.
This biotinylated lectin conjugate is prepared from affinity-purified lectin and is optimally labeled with biotin. Essentially free of inactive lectin conjugate and containing no free biotin, this biotinylated lectin provides an ideal intermediate for examining glycoconjugates using the Biotin-Avidin System. First the biotin-labeled lectin is added, followed by the VECTASTAIN® ABC Reagent, Avidin D conjugate, or streptavidin derivative. Another possible application is in the isolation of lymphokines and other products of mitogenic stimulation.