Affinity purified VRA agglutinates rabbit blood cells and is galactose-specific. Amino acid analysis of the purified mung bean lectin by reverse phase HPLC revealed that it contains glutamate in highest proportion followed by aspartate and histidine, indicating that it has a good zinc binding potential. Binding VRA with zinc improves overall stability and efficacy of the lectin.Cy5, when bound to Vigna radiata Lectin (VRA), 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 overlap 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.