Affinity purified Ulex europaeus agglutinin (UEA II) is isolated from gorse seeds and separated from crude extract. This lectin is a glycoprotein that consists of four 24,000 Da monomer subunits that require Ca2+ for binding to its ligands through carbohydrate recognition domain. It is specific for di-N-acetylchitobiose, an oligomer of GlcNAc. The monosaccharide GlcNAc is not an inhibitor of the lectin activity. UEA II has no mitogenic activity and agglutinates type O erythrocytes with greater interest than type A3 erythrocytes. Addition of EDTA eliminates agglutinating activity. Agglutinating activity can be recovered with the addition of calcium.UEA II is a potent inhibitor of the lectin complement pathway following endothelial oxidative stress. The molecular mechanism of UEA II-induced inhibition of the lectin complement pathway appears to be through competition for a common binding site on the endothelial cell and not at the level of mannose-binding lectin (MBL) inhibition. See other UEA II conjugates.SeparoporeÂ® macrobeads are larger size (160-250 micron) than average agarose beads that facilitate coupling of cells and organelles and enzymes. Affinity-purified Ulex europaeus Lectin (UEA II) was immobilized on 4% agarose macrobeads with proper configuration and stability of the lectin.