Allium sativum lectin (ASA) is purified first with affinity chromatography and then with gel filtration. It is a dimer of two subunits. ASA binds to a number of Î±1-2-linked mannose residues. The lectin recognizes internal mannose and binds to the core pentasaccharide of N-linked glycans. In addition, the removal of sialic acids enhances binding activity. Affinity purified Allium sativum Lectin (ASA) is immobilized to SeparoporeÂ® 4B following CNBr coupling. The final product is stabilized in a buffer to retain maximum activity. The gel can be packed in 1 mL or 5mL.