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Unlike Ulex europaeus and Lotus tetragonolobus lectins which prefer (α -1,2) linked fucose residues, Aleuria aurantia lectin binds preferentially to fucose linked (α -1,6) to N-acetylglucosamine or to fucose linked (α -1,3) to N-acetyllactosamine related structures. AAL also reversibly binds fucose attached to nucleic acids.
Biotinylated Aleuria Aurantia Lectin has an appropriate number of biotins bound to provide the optimum staining characteristics for this lectin. This conjugate is supplied essentially free of unconjugated biotins and is preserved with sodium azide.
| Unit Size | 1 mg |
|---|---|
| Applications | Immunohistochemistry / Immunocytochemistry, Immunofluorescence, Blotting Applications, Elispot, ELISAs, Glycobiology |
| Recommended Storage | 2-8 °C; Store frozen for long term storage |
| Inhibiting and/or Eluting Sugar | 100-400 mM L-fucose |
| Solution | 10 mM HEPES, pH 7.5, 0.15 M NaCl, 0.08% sodium azide |
| Concentration | 2 mg active conjugate/ml |
| Conjugate | Biotinylated |
| Sugar Specificity | Fucose, Arabinose |
From our experience we have found that some lectins require Ca++ to be present for optimal binding activity. We suggest using calcium chloride (CaCl2) to fortify working solutions and ensure a minimum level of Ca++ is met. This may be particularly pertinent if using phosphate based buffers as diluents and storage solutions.
This lectin is a dimer of two identical subunits of about 36 kDa each.
This biotinylated lectin is an ideal intermediate for examining glycoconjugates using the Biotin-Avidin/Streptavidin System. First the biotinylated lectin is added, followed by the VECTASTAIN ABC Reagent, Avidin D conjugate, or streptavidin derivative.
Inhibiting/Eluting Sugar: 100 mM L-fucose
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