Concanavalin A Lectin (Con A) - Biotinylated

Concanavalin A Lectin (Con A) is isolated from jack beans (Canavalia ensiformis) and purified by affinity chromatography. Con A is composed of identical subunits of 237 amino acid residues (MW: 26,000 without any cystine residues) and while above pH 7 it is predominantly tetrameric, at pH 4.5 - 5.6, Con A exists as a single dimer MW: 53,000. Con A binds with non-reducing α-D-glucose, α-D-mannose and α-methyl-D-glucopyranoside acts as a competitive inhibitor. It has a carbohydrate specificity towards α-mannose and α-glucose and elutes with MeαMan + MeαGlc. Con A does not have a blood group specificity. It exhibits mitogenic activity with lymphocytes and cancer cells which aggregate by Con A (normal white cells do not). Normal cells react to Con A after proteolytic treatment which suggests that trypsinization causes clustering of the reactive glycan residues on the membrane.  Biotin is a small molecule involved in various metabolic processes. It forms a complex with Avidin and Streptavid