Concanavalin A (Con A) derived from Canavalia ensiformis (jack bean) is a plant lectin protein (Mw 104 kDa) Under pH 7 0 Con A exists as a homotetramer composed of four subunits of 26 kDa each Under pH 4 5-5 5 Con A dissociates into active dimers (52 kDa) Acetylation succinylation or other chemical modifications can also produce stable dimeric forms Each subunit is capable of binding one Ca2 and one Mn2 and contains a carbohydrate-binding site After binding metal ions Con A can specifically bind to glycoproteins glycolipids and carbohydrate moieties containing -D-glucose and -D-mannose It is used for carbohydrate analysis glycoprotein purification enzyme tagging cell membrane studies cell agglutination assays cell cultures and cell typing This product is a ready-to-use aqueous buffered solution (500X concentrate) of Con A and serves as an exogenous lectin suitable for use as a potent leukocyte mitogen