Euonymus europaeus lectin or agglutinin (EEL/EEA) is affinity purified and is a homodimer consisting of subunits of 17 kDa linked by disulfide bonds. EEL consists of six closely related lectins (isoforms). Previous reports of higher molecular weight and overestimated carbohydrate percentage are attributed to lectin-glycoprotein complexes and not the Euonymus europaeus lectin itself. This lectin is characteristic of its erythrocyte agglutinating properties and specificity for blood groups B and H. It has a stronger binding of the B oligosaccharide with higher affinity for B-type II in comparison to H structures with Galα1,3 structures. Conversely, it has also been reported that EEL has preferential binding to H blood group-related carbohydrates over the B bloof group due to similarities in the β-trefoil fold found in EEL and ricin B-like lectins. EEL’s general pattern allows it to interact with both α-fucose 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 murine peritoneal lymphoid cells. EEL also has applications as a endothelial/epithelial marker in canine tissues and has been studied in Kashin-Beck disease. Cy3 can be used to visualize the binding pattern of EEL in cellular imaging and flow cytometry. Cy3 is more photostable than many other fluorophores and can be seen with TRITC filter sets. It is commonly combined with green-fluorescent dyes for dual-labeling. This product comes in a stabilized liquid form.
Source Euonymus europaeus (Spindle tree)
Activity: 50 mg/ml will agglutinate human A2 erythrocytes.
Carbohydrate Specificity: Galα3Gal, high mannose N-type glycans
Inhibitory Carbohydrate: Lactose
Divalent Ions Required: Ca++, Zn++
Storage and Stability:
Store frozen at -20°C in amber vials or covered with foil in appropriate aliquot sizes. Avoid freeze thaw cycles. Can be stored at 2-8 °C for short term use. Clarify by centrifugation, if needed.