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.
Alkaline phosphatase (AP) is conjugated to Lycopersicon esculentum Lectin (LEL/LEA) to show the binding of LEL/LEA in many applications including Western blotting and ELISA. Alkaline phosphatase is a large protein (140 kDa) that catalyzes the hydrolysis of phosphate groups from a substrate resulting in a colored or fluorescent product. The optimal enzymatic activity of this protein is between pH 8 and 10, and its reaction rate remains linear, improving sensitivity over time.