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 as part of the receptor structure. 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 unconjugated form is supplied as a solution preserved with sodium azide. The recommended inhibiting/eluting sugar is a mixture of 200 mM α-methylmannoside/200 mM α-methylglucoside.