Concanavalin A is a pure Canavalia ensiformis lectin, FITC conjugated proteins or glycoproteins of non-immune origin that agglutinate cells and precipitate complex carbohydrates. They are capable of binding glycoproteins even in presence of various detergents.

• Carbohydrate specificity: a-mannose, a-glucose, branched Mannose
• Inhibitory carbohydrate: Methyl-a-D-mannopyranoside>>a-D-mannose>>a-D-glucose

It is not blood group specific but has an affinity for terminal α-D-mannosyl and α-D-glucosyl residues. Ca²⁺ and Mn²⁺ ions are required for activity. It dissociates into dimers at pH 5,6 or below. Between pH 5,8 and pH 7,0, it exists as a tetramer; above pH 7,0 higher aggregates are formed. It exhibits mitogenic activity which is dependent on its degree of aggregation.

It is used to examine tissue sections. It is conjugated to FITC, allowing fluorescent detection in binding assays for example detection of glycoproteins containing α−D-mannose or α−D-glucose. It is also used in blood grouping and erythrocyte polyagglutination studies, mitogenic stimulation of lymphocytes, lymphocyte subpopulation studies, fractionation of cells and other particles, histochemical studies of normal and pathological conditions.