Concanavalin A Lectin (Con A) - Cy5

Concanavalin A Lectin (Con A) is isolated from jack bean seeds (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. This product comes in a stable lyophilized form. Cy5, when bound to Con A, can show the binding pattern of this lectin in cellular imaging and flow cytometry. The excitation wavelength required for Cy5 to fluoresce is high enough to avoid overlapping with most other fluorochromes, making it useful for dual-labeling experiments. Because of this high excitation, there is typically less background from autofluorescence of biological specimens.

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, Bioconjugations, ELISA, ELLA, Western Blot, Cancer research & Therapeutics, In vivo modeling, 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.