Wheat germ agglutinin (WGA) is a well-studied lectin known for its binding affinity to N-acetyl-D-glucosamine and sialic acid, making it a valuable tool in various biological applications. Its interaction with glycoconjugates enables widespread use of WGA derivatives and conjugates for fluorescence imaging and analysis, facilitating the labeling of yeast bud scars, fibrotic scar tissue, and the cell membranes of gram bacteria and mammalian cells. WGA specifically targets sequences of β-1,4-GlcNAc-linked residues known as chitodextrins. Each monomer contains two identical, non-interacting binding sites complementary to 3 or 4 β-1,4-GlcNAc units. Among the monosaccharides tested, only GlcNAc shows strong binding to WGA, while ManNAc demonstrates no binding, and GalNAc exhibits weak binding. The iFluor® 532 conjugate of WGA possesses a bright, red fluorescence characteristic of the iFluor® 532 dye (Ex/Em = 537/560 nm). Notably, the iFluor® 532 WGA conjugate, like Alexa Fluor® 532 WGA conjugate, retains its ability to bind to sialic acid and N-acetylglucosaminyl residues, enhancing its utility in fluorescence imaging and analysis for various scientific investigations.