Allium sativum lectin (ASA) is purified by separation followed by gel filtration. It is a dimer of two subunits. ASA binds to a number of -1-2 linked mannose residues. Lectins recognize internal mannose and bind to the core five sugars of N-chain glycans. In addition, the removal of sialic acid enhances the binding activity.
For research use only, not for clinical use.