Ulex europaeus Lectin (UEA I) - Alexa Fluor 647

Ulex europaeus agglutinin (UEA I) is affinity-purified from gorse seeds and separated from crude extract using affinity chromatography. Composed of two subunits, this glycoprotein has no mitogenic activity and primarily agglutinates type O erythrocytes, with lesser activity toward A2 erythrocytes. UEA I exhibits strong reactivity with α(1,2)-linked fucose residues but minimal or no binding to α(1,3) or α(1,6)-linked fucose. It cannot bind internal fucose structures, and the presence of an internal α(1,3)-linked fucose on H type 2 oligosaccharides reduces lectin affinity for this blood group antigen by three-fold. UEA I has been utilized as a marker for vascular endothelium and to identify endothelial cells in benign vascular lesions more specifically than Factor VII-related antigen antibodies. Additionally, UEA I-coated magnetic beads are employed to isolate endothelial cells associated with micro-vessels for cell culture and to differentiate between angiosarcomas and epithelial tumors.

Ulex europaeus Lectin conjugated with Alexa Fluor™ 647 is a bright, far red fluorescent dye with excitation ideally suited for the 633 nm laser line. This dye is designed for stable signal generation in imaging and flow cytometry, providing reliable detection capabilities. Alexa Fluor™ 647 is water soluble and maintains pH insensitivity from pH 4 to pH 10, ensuring versatility in a wide range of experimental settings. This conjugate enhances the sensitivity and precision of cellular labeling, making it an excellent choice for research applications.

Recommended usage: Recommended dilutions of 5 – 10 μg/ml in 20 mM Tris-HCl pH 7.5 with 50 mM NaCl, 1 mM CaCl2, 0.5 mM MnCl2. To prevent degradation and avoid repeated freeze-thaw cycles, aliquot your product into small, single-use volumes and store them at -20⁰C.

Application

Immunofluorescence, Immunohistochemistry, Immunocytochemistry, Biomarker, Cell sorting, Blotting, ELISA, Glycobiology.

References

1. Allen HJ, Johnson EA. A simple procedure for the isolation of L-fucose-binding lectins from Ulex europaeus and Lotus tetragonolobus. Carbohydr Res. 1977 Oct;58(2):253-65.
2. Loris R, De Greve H, Dao-Thi MH, Messens J, Imberty A, Wyns L. Structural basis of carbohydrate recognition by lectin II from Ulex europaeus, a protein with a promiscuous carbohydrate-binding site. J Mol Biol. 2000 Aug 25;301(4):987-1002.