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.
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 Euonymus europaeus Lectin (EEL/EEA) 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.