Euonymus europaeus Lectin (EEL/EEA) - Biotinylated

europaeus Euonymus lectin (EEL/EEA) is an affinity-purified homologous dimer consisting of a 17kda subunit linked by a disulfide bond. EEL consists of six closely related lectins (isomers). Previously reported higher molecular weights and overestimated carbohydrate percentages are attributed to the lectin-glycoprotein complex, rather than Euonymus lectins themselves. The lectin has erythrocyte agglutination properties and specificity for B and H blood types, and it binds more strongly to B oligosaccharides and has a higher affinity for B type II than the H structure with the gal α1,3 structure. Conversely, it has also been reported that EEL preferentially binds to carbohydrates associated with blood group H over blood group B due to the similarity of the β-triloba fold in EEL and ricin B-like lectins. The general pattern of EEL allows it to interact with α-focusing residues on B and H blood groups, as well as high-mannose N-type glycans. This lectin binds to endothelial cells from human and non-human sources and recognizes carbohydrate structures on the surface of stimulated mouse peritoneal lymphoid cells. EEL has also been used as an endothelial/epithelial marker in canine tissues and has been studied in Kashin-beck disease. Biotin is a small molecule involved in a variety of metabolic processes. This ligand forms complexes with avidin and streptavidin, resulting in the strongest known non-covalent protein-ligand interaction. Biotinylated EEL has the right amount of biotin binding to provide the best detection characteristics when using avidin-HRP or streptavidin-HRP couplings. Biotinylated lectins allow for more sensitive detection in ELISA and Western-blotting applications.