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.
Lycopersicon esculentum Lectin (LEL/LEA) is conjugated to ferritin, that has a molecular weight of 474,000 g/mol (all 24 subunits combined). Ferritin-conjugated lectins can be used to visualize localization of specific saccharide moieties and examine the distribution of plasma membrane glycoproteins. These conjugates can be viewed via electron microscopy.