Concanavalin A, MP Biomedicals™

Lectin are used in a wide variety of applications. Con-A is not a glycoprotein and does not contain cysteine residues. Unlike most other lectins, Con-A is a metalloprotein and requires a transition metal ion, such as manganese, plus calcium ions for binding.

• Con A is not blood group specific but has an affinity for terminal α-D-mannosyl and α-D-glucosyl residues. Con-A binds specifically to mannosyl and glucosyl residues of polysaccharides and glycoproteins.
• Unmodified hydroxyl groups at the C3, C4 and C6 positions of D-glucopyranosyl or D-mannopyranosyl rings may be essential for binding.
• Each subunit of Con A contains one calcium ion and one manganese ion. Removal of these cations by dialysis under acidic conditions abolishes the carbohydrate-binding 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.