Datura Stramonium Lectin (DSL), Biotinylated

Carbohydrate-binding site recognition (beta-1,4) -linked N-acetylglucosamine oligomers favored chitosan or chitosaccharides over individual n-acetylglucosamine residues. The lectin binds well in the acidic pH range, but its affinity decreases above pH 8.0. DSL also binds well to N-acetyllactamine and oligomers containing repeated n-acetyllactamine sequences. A branched-chain pentasaccharide consisting of two n-acetyllactodicosse-linked mannose (beta-1,6) and (beta-1,2) has been reported to be the most potent agglutination inhibitor. Biotinylated mandala lectins bind the appropriate amount of biotin to provide the best staining properties for the lectins. This conjugate contains essentially no unconjugated biotin and is preserved with sodium azide.