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. Cy3 can be used to viualize the binding pattern of Allium sativum Lectin (ASA) in cellular imaging and flow cytometry. Cy3 is more photostable than many other flourophores and can be seen with TRITC filter sets. It is commonly combined with green-fluorescent dyes for dual-labeling.