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 Î±(1,2) linked fucose residues but poorly or not at all with Î±(1,3) or Î±(1,6)-linked fucose. UEA I is unable to bind internal fucose structures and the presence of an internal Î±(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.Alkaline phosphatase (AP) is conjugated to Ulex europaeus Lectin (UEA I) to show the binding of UEA I 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.