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 α1-2-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.
Allium sativum Lectin (ASA) is labeled with tetramethylrhodamine isothiocyanate (TRITC) and has an appropriate number of fluorochromes bound to provide the optimum staining characteristics for this lectin. TRITC is a bright orange or red-fluorescent dye with excitation ideally suited to the 532-nm laser line. TRITC labeled ASA can be used for cellular imaging applications.