Allium sativum Lectin (ASA) - Pure

Product Description
Lectin ASA is isolated from garlic bulbs (Allium sativum) and purified by affinity chromatography, followed by gel filtration. ASA is a heterodimer of two subunits with a molecular weight of 24,000. The lectin's sugar specificities can be elucidated by hemagglutination inhibition and a coupled enzyme-based assay. The hemagglutination inhibition study helps confirm this lectin’s specificity for D-mannose, while a sensitive enzyme-based assay can examine detailed binding specificities. Binding sites of ASA accommodate a number of a1-2-linked mannose residues, with an elution concentration of 0.2M of mannose. Interaction with glycoproteins not only suggests that the lectin recognizes internal mannose but that also binds to the core pentasaccharide of N-linked glycans even when it is sialylated. Although the binding site can withstand terminal sialic acids and the penultimate galactose residues, the removal of sialic acids enhances potency. ASA shows blood group specificity towards rabbit erythrocytes and weak interaction with human erythrocytes.

ASA comes in lyophilized powder form and is stored below -20 C.

Applications:
Agglutination studies


References

• Anita G. A new high molecular weight agglutinin from garlic (Allium sativum). Mol Cell Biochem. (1997) 166:1-9.
• Dam, T., et al. Garlic (Allium sativum) Lectins Bind to High Mannose Oligosaccharide Chains. J Biol Chem. (1998) 273:5528-35.
• Tarun D. Garlic (Allium sativum) Lectins Bind to High Mannose Oligosaccharide Chains. J Biol Chem. (1998) 273:5528-35.