Allium sativum Lectin (ASA) - Cy5

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. 

Cy5, when bound to Allium sativum Lectin (ASA), can show the binding pattern of this lectin in cellular imaging and flow cytometry. The excitation wavelength required for Cy5 to fluoresce is high enough to avoid overlapping with most other fluorochromes, making it useful for dual-labeling experiments. Because of this high excitation, there is typically less background from autofluorescence of biological specimens.

Application: Immunofluorescence, Immunohistochemistry, Immunocytochemistry, Anti-cancer, Glycobiology.

Recommended usage: 1XPBS can be used for reconstitution/dilution. Recommended dilution range is 0.5-10 µg / ml.

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