Euonymus europaeus Lectin (EEL/EEA) - Pure

Product Description
Euonymus europaeus lectin or Euonymus europaeus agglutinin (EEL/EEA) is isolated from the spindle tree (Euonymus europaeus) and purified by affinity chromatography. EEL has a molecular weight of 140,000 with most of the subunits that appear to consist of two chains linked by disulfide bonds. EEL consists of six closely related lectins (isoforms) with isoelectric points between pH 4.3 and pH 4.7.

EEL adopts a Beta-trefoil fold, similar to ricin B-like (R-type) lectins. Identified γ binding site has been found to be the primary carbohydrate-binding site of EEL. The γ site features a solvent-exposed tryptophan residue (Trp143) that appears to be involved in CH-π interactions with the ligands.

EEL is a carbohydrate-binding protein, first identified for its erythrocyte agglutinating properties and specificity for blood groups B and H. Studies have shown a stronger binding of the H trisaccharide over the B trisaccharide, but with general pattern of EEL 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, and elutes a concentration of 0.2M of lactose. EEL has been reported to bind to endothelial cells from human and non-human sources, and recognizes carbohydrate structures on the surface of stimulated murine peritoneal lymphoid cells.

EEL product comes in a lyophilized powder form and is stable for 12 months stored at -20 C. Reconstitute with sterile buffer, reconstituted product is stable for 6 months at -20 C. Metal ions calcium and zinc are required for binding.

Applications:
Suitable for use in ELISA

References

• Agostino, M. The carbohydrate-binding promiscuity of Euonymus europaeus lectin is predicted to involve a single binding site. Glycobiology. (2015) 25:101-114.