Datura stramonium agglutinin or lectin (DSA/DSL) is purified by affinity chromatography. Seeds of Datura stramonium contain at least three different carbohydrate-binding proteins, and the most prominent lectin is a dimeric glycoprotein composed of two non-identical subunits that contains 40% carbohydrate. It binds well to N-acetylglucosamine, oligomers, and branched pentasaccharide, including two N-acetylglucosamine disaccharides linked to mannose (β-1,6) and (β-1,2), which is known to be the most potent inhibitor of agglutination. DSL prefers binding to (GlcNAc)2-4 and elutes with the sugar chitin hydrolysate. DSL binds well in the acidic pH range and its affinity decreases above pH 8.0. This agglutinin has blood group A, B, and O specificity. Studies have shown that DSA can act as a biomarker for neoplastic urothelial cells.

Recommended Usage: Recommended dilutions of 0.5 – 10 µg/ml in 1XPBS. Human O erythrocytes will agglutinate by 20 – 30 µg/ml of DSA.

Storage Instruction: To prevent degradation and avoid repeated freeze-thaw cycles, aliquot your product into small, single-use volumes and store them at -20°C

Application

Western blotting, Mitogenic stimulation, ELISA, ELISPOT, Immunohistochemistry, Immunocytochemistry, Antiproliferative, Glycobiology.

References

1.Nishimoto K, Tanaka K, Murakami T, Nakashita H, Sakamoto H, Oguri S. Datura stramonium agglutinin: cloning, molecular characterization and recombinant production in Arabidopsis thaliana. Glycobiology. 2015 Feb;25(2):157-69.
2.Hirabayashi J, Lectin Purifications and analysis. Book. 2020. Methods in Molecular Biology (MIMB, volume 2132).
3.Kilpatrick DC, Yeoman MM. Purification of the lectin from Datura stramonium. Biochem J. 1978 Dec 1;175(3):1151-