Allium sativum Lectin (ASA) - TRITC (Rhodamine)

Allium sativum lectin (ASA) is isolated from garlic bulbs and purified with affinity chromatography. It is a dimer of two subunits. ASA binds to several 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. The binding site can withstand terminal sialic acid and galactose residues. The blood group specificity of ASA is towards rabbit erythrocytes and weak interaction with human erythrocytes. 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.

Recommended Usage: Recommended dilutions ratio to use from 0.5 – 10 µg / ml. 1XPBS pH 7.4 can be used as dilution buffer. Les than 0.5 µg / ml will agglutinate rabbit erythrocytes.

Storage Instruction: To prevent degradation and avoid repeated freeze-thaw cycles, aliquot your product into small, single-use volumes and store them at -20°C

Application

Immunocytochemistry, Immunohistochemistry, Immunofluorescence, Glycobiology

References

1. Ghosh, P., Sen, S., Chakraborty, J., & Das, S. (2016). Monitoring the efficacy of mutated Allium sativum leaf lectin in transgenic rice against Rhizoctonia solani. BMC biotechnology, 16, 24.

2. Kumar, S., Jitendra, K., Singh, K., Kapoor, V., Sinha, M., Xess, I., Das, S. N., Sharma, S., Singh, T. P., & Dey, S. (2015). Biological Properties and Characterization of ASL50 Protein from Aged Allium sativum Bulbs. Applied biochemistry and biotechnology, 176(7), 1914–1927.