Lens culinaris agglutinin (LCA) contains two subunits of 17 kDa and two of 8 kDa. It has a narrower specificity than ConA because it recognizes sequences containing α-linked mannose residues and other sugars. An α-linked fucose attached to the N-acetylchitobiose of the core oligosaccharide enhances affinity. The narrower specificity allows subfractionation of glycoproteins and peptides after initial isolation with Con A. LCA prevents skin allograft rejection and can purify numerous glycoproteins, including immunoglobulins, histocompatibility antigens, and α2-macroglobulin. This conjugate of LCA to Dylight 649 features a ratio of fluorophore to lectin protein that provides optimal staining (excitation 655 nm, emission 670 nm). Supplied as a solution essentially free of unconjugated fluorophore, it is preserved with sodium azide. The recommended inhibiting/eluting sugar is a mixture of 200 mM α-methylmannoside/200 mM α-methylglucoside.