Concanavalin A from Canavalia ensiformis (Jack bean)

Concanavalin A is isolated from the from Canavalia ensiformis (Jack bean). It is a mitogenic lectin with a dome-like structures and is a tetrameric protein.

Concanavalin A from Canavalia ensiformis (Jack bean) has been used:

• in the colabelling of fischer rat thyroid (FRT) epithelia(104)
• to induce autoimmune hepatitis in Cre-conditional atg7 knockout mice(105)
• to detect glycoproteins containing α-D-mannose, α-D-glucose when used with avidin or streptavidin detection system(106)

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) bound to glycoenzyme has wide applications and can be dissociated in the presence of high sugar levels. Con A induces hepatic inflammation. It stimulates macrophages and promotes cytokine production. Con A also exhibits anti-hepatoma effect and could be used effectively as a vaccine for treating cancer.

Package size based on protein content

Contains sodium citrate

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.