Concanavalin A from Canavalia ensiformis (Jack bean)

Concanavalin A from Canavalia ensiformis (Jack bean) has been used for developing zwitterion-immobilized molecularly imprinted polymers (ziMIPs) for protein crystallization. It has been also used in the preparation of protein loaded microgels to prevent enzymatic degradation of microgels for monitoring by confocal laser scanning microscope (CLSM).

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.

Highly purified by specific affinity chromatography.

Agglutination activity: Determined from serial dilutions of a 1 mg/mL solution (this activity is the lowest conc. to agglutinate a 2% suspension of human erythrocytes after 1 hr incubation at 25 °C). Requires Type A Human Blood.