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. Fluorescein-labeled DSLS have the appropriate amount of fluorescent dye binding to provide the best staining properties for this lectin. This conjugated substance basically does not contain unconjugated fluorescent dyes. The excitation maximum is 495nm and the emission maximum is 515nm.
For research use only, not for clinical use.