L7400
Lectin from Euonymus europaeus (spindle tree)
lyophilized powder
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About This Item
UNSPSC Code:
12352200
MDL number:
form
lyophilized powder
potency
<1 μg per mL (using neuraminidase-treated Type B red blood cells.)
composition
Protein, ~5% Lowry
storage temp.
−20°C
General description
Euonymus europaeus lectin (EEL) is a carbohydrate-binding protein. derived from the fruit of the European spindle tree. Lectin, obtained from the fruit of the European spindle tree, called E. europaeus possesses high tolerance.
Biochem/physiol Actions
Euonymus europaeus agglutinin (EEA) has anti-B+H blood group specificity and is reported to be most specific for blood group B oligosaccharides having the structure α-D-Gal(1→3)[α-L-Fuc(1→2)]-β-D-Gal(1→3/4)-β-D-GlcNac, The B+H specificity is an intrinsic property of a single lectin binding site. Lectin from Euonymus europaeus successfully binds to several carbohydrates, such as, a series of blood group-related carbohydrates, mannosides, chitotriose and sialic acid. EEL recognizes the carbohydrates terminating in several monosaccharides by using a single site.
Physical form
Lyophilized powder containing sodium chloride and phosphate buffer salts
Analysis Note
Agglutination activity is expressed in μg/mL and is determined from serial dilutions in phosphate buffered saline, pH 7.2, of a 1 mg/mL solution. This activity is the lowest concentration of lectin to agglutinate a 2% suspension of neuraminidase-treated human blood group B erythrocytes after 1 hr incubation at 25 °C.
Storage Class
13 - Non Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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The carbohydrate-binding promiscuity of Euonymus europaeus lectin is predicted to involve a single binding site
Agostino M, et al.
Glycobiology, 25(1), 101-114 (2014)
Studies on Gal-beta 3-binding proteins: comparison of the glycosphingolipid binding specificities of Marasmius oreades lectin and Euonymus europaeus lectin
Teneberg S, et al.
Glycobiology, 13(6), 479-486 (2003)
Nirupam Purkayastha et al.
Chemistry & biodiversity, 12(2), 179-193 (2015-02-14)
β(3) -Octaarginine chains were attached to the functional groups NH and CO2 H of the antibacterial fluoroquinolones ciprofloxacin (→1) and enrofloxacin (→2), respectively, in order to find out whether the activity increases by attachment of the polycationic, cell-penetrating peptide (CPP)
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