Concanavalin A (from Jack Bean), MP Biomedicals
Supplier: TestTotal Ratings: 0
Avg. Ratings: 0.0 out of 5
Pure Canavalia ensiformis lectin (Con A) from Jackbean. Isolated by affinity chromatography on cross-linked dextran. Con A exists as a dimer below pH 5.0 and and at pH >7 it exists as a tetramer. Con-A is not a glycoprotein. The monomeric molecular weight of Con-A is 25500. Con-A 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.
- Isoelectric point (pl): 4.5, 4.7, 5.0 to 5.1, and 5.4 to 5.5 (several isoforms)(Lit.)
- Inhibitory Carbohydrate: Methyl-a-D-Mannopyranoside >> a-D-Mannose >> a-D-Glucose
- Carbohydrate Specificity: a-Mannose, a-Glucose, Branched Mannose
- Soluble in water (10 mg/ ml-slightly hazy, colorless solution)
- GHS symbols and signal word: GHS07, GHS08 and Danger
Lectin are used in a wide variety of applications in vitro, including: 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. Con-A has been used to elucidate structural changes in the membrane surface of transformed cells. Con-A conjugates of antitumor drugs have been used in drug delivery systems in cultured cells.
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. 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.
Inhibitory Carbohydrate: Methyl-a-D-Mannopyranoside
Learn more
About VWR
Avantor is a vertically integrated, global supplier of discovery-to-delivery solutions for...