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 Streptavidin, resulting in the strongest non-covalent protein-ligand interaction known. Biotinylated Concanavalin A (Jackbean) lectin (Con A) has an optimal amount of biotin bound for effective detection when using an Avidin-HRP or Streptavidin-HRP conjugate. Biotinylated lectins enable more sensitive detection in ELISA and Western blotting applications.

Recommended Usage: Recommended dilutions of 0.5-10 µg in 0.5 M Sodium Phosphate Buffer pH 7.4. More than 10ug/ml may be required to give visible agglutination of neuraminidase treated human erythrocytes.

Storage Instruction: To prevent degradation and avoid repeated freeze-thaw cycles, aliquot your product into small, single-use volumes and store them at -20°C

Application

Immunohistochemistry, Immunocytochemistry, Immunofluorescence, ELISA, Western Blotting, Cell typing, T cells proliferation assays, Chromatin profiling, Glycobiology.

References

1.Darmani H, Coakley WT. Contact patterns in concanavalin A agglutinated erythrocytes. Cell Biophys. 1991 Feb;18(1):1-13.
2.Olson MO, Liener IE. Some physical and chemical properties of concanavalin A, the phytohemagglutinin of the jack bean. Biochemistry. 1967 Jan;6(1):105-11.
3.McCubbin WD, Kay CM. Molecular weight studies on concanavalin A. Biochem Biophys Res Commun. 1971 Jul 2;44(1):101-9.