Overview
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.
| Cat. No. |
L-1180-5 |
| Unit Size |
5 mg |
| Country of Manufacture |
United States |
| Applications |
Glycobiology, Mitogenic Stimulation |
| Conjugate |
Unconjugated |
| Sugar Specificity |
[GlcNAc]1-3, N-Acetylglucosamine |
More Information
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.
Inhibiting/Eluting Sugar: Chitin Hydrolysate
Protocols/Data Sheets/SDS
