Affinity purified Euonymus europaeus lectin or agglutinin (EEL/EEA) is composed with most of the subunits that appear to consist of two chains linked by disulfide bonds. EEL consists of six closely related lectins (isoforms). EEL is identified for its erythrocyte agglutinating properties and specificity for blood groups B and H. It has a stronger binding of the H trisaccharide over the B trisaccharide, but has a general pattern of interacting with both B and H blood groups and α-mannose-terminated saccharides. EEL has a preferential recognition of terminal α-fucose residues in H and B blood group-related carbohydrates. This lectin binds to endothelial cells from human and non-human sources and recognizes carbohydrate structures on the surface of stimulated murine peritoneal lymphoid cells. See other EEL/EEA conjugates.
Alkaline phosphatase (AP) is conjugated to Euonymus europaeus Lectin (EEL/EEA) to show the binding of EEL/EEA 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.