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The receptor sugar for WGA is N-acetylglucosamine, with preferential binding to dimers and trimers of this sugar. WGA can bind oligosaccharides containing terminal N-acetylglucosamine or chitobiose, structures which are common to many serum and membrane glycoproteins. Bacterial cell wall peptidoglycans, chitin, cartilage glycosaminoglycans, and glycolipids can also bind WGA. Native WGA has also been reported to interact with some glycoproteins via sialic acid residues (see succinylated WGA).
Rhodamine labeled WGA has an appropriate number of fluorochromes bound to provide the optimum staining characteristics for this lectin. This conjugate is supplied essentially free of unconjugated fluorochromes. The excitation maximum is at 550 nm and the emission maximum is at 575 nm.
| Unit Size | 5 mg, 10 mg |
|---|---|
| Applications | Immunofluorescence, Glycobiology |
| Recommended Usage | For most applications we recommend a freshly prepared working solution of 5-20 µg/mlin the above buffer. |
| Recommended Storage | 2-8 °C |
| Maximum Excitation | 545-555 nm |
| Inhibiting and/or Eluting Sugar | 400 mM N-acetylglucosamine (S-9002) |
| Maximum Emission | 570-580 nm |
| Solution | 10 mM HEPES, 0.15 M NaCl, pH 7.5, 0.08% sodium azide, 0.1 mM CaCl2, 25 mM N-acetylglucosamine |
| Concentration | 5 mg active conjugate/ml |
| Conjugate | Rhodamine |
| Sugar Specificity | N-Acetylglucosamine |
Wheat germ agglutinin (WGA) contains a group of closely related isolectins, with an isoelectric point about pH 9. This lectin is used for the purification of insulin receptors.
Accompanying each fluorescent lectin is an analysis data sheet summarizing the results of our quality control tests and providing pertinent information on the product. All of these reagents are supplied as solutions preserved with sodium azide.
Inhibiting/Eluting Sugar: Chitin Hydrolysate or 500 mM N-acetylglucosamine with salt and/or acid elution generally required
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