Ulex europaeus agglutinin (UEA I) is affinity purified isolated from gorse seeds and separated from crude extract by affinity chromatography. It is consists of two subunits. The lectin is a glycoprotein that has no mitogenic activity to agglutinates type O erythrocytes, and of a lesser degree to individuals with A2 erythrocytes.
UEA I reacts strongly with α(1,2) linked fucose residues but poorly or not at all with α(1,3) or α(1,6)-linked fucose. UEA I is unable to bind internal fucose structures and the presence of an internal α(1,3)-linked fucose on the H type 2 oligosaccharide decreases lectin affinity for this blood group antigen by 3-fold.
UEA I has been used as a marker for vascular endothelium and used to identify endothelial cells of benign vascular lesions more specifically than antibodies Factor VII-related antigen. UEA I coated magnetic beads have been used to isolate endothelial cells associated with micro-vessels for subsequent cell culture. This lectin has also been used to differentiate between angiosarcomas and epithelial tumor.
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 Ulex europaeus Lectin (UEA I) 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.