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.
Biotin is a small molecule involved in a wide range of metabolic processes. This ligand forms a complex with Avidin and Streptavidin, resulting in the strongest non-covalent protein-ligand interaction known. Biotinylated Phaseolus limensis Lectin (LBA) has an appropriate amount of biotin bound to provide optimum detection characteristics when using an Avidin-HRP or Streptavidin-HRP conjugate. Biotinylated lectins allow for more sensitive detection in ELISA and Western-blotting applications.