Allium sativum lectin (ASA) is isolated from garlic and purified with affinity chromatography. 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. ASA has shown antiproliferative and apoptosis-inducing activity, making it a relative subject in cancer research.
Purified ASA is labeled with Tetramethylrhodamine isothiocyanate (TRITC) and comes in a stabilized liquid form. TRITC is a bright orange or red-fluorescent dye with excitation ideally suited to the 532-nm laser line. It has an excitation maximum at 546 nm and an emission maximum at 569 nm. Conjugated form of TRITC is used for cellular imaging applications.
• Source: Allium sativum Lectin (Garlic) ASA
• Activity: Agglutinates rabbit but not human erythrocytes
• Protein Concentration (Based on OD 280): 1 mg purified ASA TRITC/1 mL buffer
• Conjugation: TRITC (Rhodamine)
• Carbohydrate Specificity: Mannose
• Inhibitory Carbohydrate: α(1,3) linked mannosyl units
• Fluorescence: Red-Orange fluorescent
• Excitation: Maximum at 545-55 nm
• Emission: Maximum at 570-580 nm
Storage and Stability:
Store frozen at -20°C in amber vials or covered with foil in appropriate aliquot sizes. Avoid freeze thaw cycles. Can be stored at 2-8°C for short term use. Clarify by centrifugation, if needed.