Succinylated wheat germ agglutinin (Succ-WGA) is affinity purified from the native wheat germ agglutinin (WGA). It is dimeric at pH as low as 5 and dissociates at pH lower than 4.5. Succ-WGA agglutinates rabbit erythrocytes at a minimal concentration of about 2g/ml, and agglutinates human erythrocytes of blood groups A, B, and O types. The solubility of Succ-WGA is around 100 times higher than the unmodified lectin at neutral pH. Ulike native WGA, Succ-WGA does not bind to sialic acid residues but retains its specificity towards N-acetylglucosamine. The use of conjugates of the native WGA and the succinylated allows to distinguish between sialylated glycoconjugates and others N-acetylglucosamine structures. See other Succ-WGA conjugates.
Cy5, when bound to Succinylated Triticum vulgaris Lectin (Succ WGA), 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.