Concanavalin A from Canavalia ensiformis (Jack bean)

Concanavalin A (Con A), isolated from Jack beans (Canavalia ensiformis), is a mannose or glucose specific-binding lectin. The lectin is a tetramer and each subunit possesses a saccharide-binding site. Con A can be isolated by affinity chromatography with dextrans.

Used for the purification of glycoproteins containing mannose

Concanavalin A (Con A) has been used for enzyme immobilization.

Con A 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. Con A dissociates into dimers at pH 5.6 or below. Between pH 5.8 and pH 7.0, Con A exists as a tetramer; above pH 7.0 higher aggregates are formed. Con A exhibits mitogenic activity which is dependent on its degree of aggregation. Succinylation results in an active dimeric form which remains a dimer above pH 5.6.

Concanavalin A (Con A) is a T cell mitogen that can activate the lymphocytes.
Con A can induce tumor cell death through autophagy.

Suspension in 1.0 M NaCl + 0.1 M potassium phosphate, pH 6.0, with 1 mM CaCl₂, 1 mM MgCl₂ and 1 mM MnCl₂ containing preservative

Where reported, agglutination activity is expressed in μg/ml and is determined from serial dilutions in phosphate buffered saline, pH 6.8, containing Ca²⁺ and Mn²⁺ of a 1 mg per mL solution. This activity is the lowest concentration to agglutinate a 2% suspension of human erythrocytes after 1 hr incubation at 25 °C.