Phaseolus limensis agglutinin (LBA) is isolated from lima bean seeds and purified by affinity chromatography. LBA is composed of 30,000 Da subunits, of which two are joined by a disulfide bond. Each subunit contains a cysteine residue which is required for both it’s carbohydrate- and metal-ion-binding activities. It has a carbohydrate specificity of terminal GalNAcα(1,3)Gal that elutes with N-acetylgalactosamine. LBA agglutinates blood group A erythrocytes.
Cy3 can be used to visualize the binding pattern of Phaseolus limensis Lectin (LBA) in cellular imaging and flow cytometry. Cy3 is more photostable than many other fluorophores and can be seen with TRITC filter sets. It is commonly combined with green-fluorescent dyes for dual-labeling.