Allium sativum Lectin (ASA) - Cy3

Allium sativum lectin (ASA) is isolated from garlic 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.  ASA has shown antiproliferative and apoptosis-inducing activity, making it a relative subject in cancer research. Cy3 can be used to visualize the binding pattern of ASA in cellular imaging and flow cytometry.

Cy3-labeled ASA is ideal for visualizing binding patterns in cellular imaging and flow cytometry. This dye offers superior photostability compared to many other fluorophores and is compatible with TRITC filter sets. Cy3 is commonly paired with green-fluorescent dyes for effective dual-labeling.

Applications: Immunocytochemistry, Immunofluorescence, Anti cancerous, Glycobiology

Recommended usage: Recommended dilution ranges 0.5 – 10 µg/ml. 1XPBS can be used for reconstitution. Less than 0.5 ug /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

References

1.Ghosh, P., Sen, S., Chakraborty, J., & Das, S. (2016). Monitoring the efficacy of utated Allium sativum leaf lectin in transgenic rice against Rhizoctonia solani. BMC biotechnology, 16, 24. https://doi.org/10.1186/s12896-016-0246-0.

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.