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.
Affinity purified Lycopersicon esculentum Lectin (LEL/LEA) is immobilized on aminated paramagnetic beads using EDC and stabilized in a buffer to retain maximum activity. These beads are ideal for iP applications to pull down glycoproteins.