Datura stramonium lectin (DSL), Fluorescein

DSL contains two chains of 40 kDa and 46 kDa joined by disulfide bonds. This lectin is free of a reported 32 kDa contaminant protein. The carbohydrate binding site recognizes (β-1,4) linked N-acetylglucosamine oligomers, preferring chitobiose or chitotriose over a single N-acetylglucosamine residue. This lectin binds well in the acidic pH range but its affinity decreases above pH 8.0. DSL also binds well to N-acetyllactosamine and oligomers containing repeating N-acetyllactosamine sequences. A branched pentasaccharide including two N-acetyllactosamine disaccharides linked to mannose (β-1,6) and (β-1,2) was reported to be the most potent inhibitor of agglutination. Fluorescein labeled DSL has an appropriate number of fluorochromes bound to provide the optimum staining characteristics for this lectin. This conjugate is supplied essentially free of unconjugated fluorochromes. The excitation maximum is at 495 nm and the emission maximum is at 515 nm. Accompanying each fluorescent lectin is an analysis data sheet summarizing the results of our quality control tests and providing pertinent information on the product. All of these reagents are supplied as solutions perserved with sodium azide. Inhibiting/Eluting Sugar: Chitin Hydrolysate.

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