Isolated from tomatoes, affinity-purified Lycopersicon esculentum lectin (LEL/LEA) has a carbohydrate specificity toward GlcNac. Composed of a single stable subunit, LEL is a useful marker of tracking vasculature in rodents and in neuroscience research. This lectin has an unusually high carbohydrate content of about 50 percent arabinose and galactose. LEL is non-specific agglutinates human erythrocytes A, B, O, or AB blood types. Protease-treated erythrocytes are slightly more sensitive to agglutination by this lectin.
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 Lycopersicon esculentum Lectin (LEL/LEA) 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.