Although the specificity of this lectin is not well defined, MAL II appears to bind only particular carbohydrate structures that contain sialic acid. Unlike Sambucus nigra lectin (SNA) which seems to prefer structures with (α-2,6) linked sialic acid, MAL II appears to bind sialic acid in an (α-2,3) linkage. Tissue staining patterns are also very different among MAL I, SNA and MAL II.
Biotinylated Maackia amurensis lectin II 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 Usage | For most applications, we recommend a freshly prepared working solution of 5-20 µg/ml in the below buffer. |
| Recommended Storage | 2-8 °C |
| Solution | 10 mM HEPES, pH 7.5, 0.15 M NaCl, 0.08% sodium azide. |
| Concentration | 1 mg active conjugate/ml |
| Conjugate | Biotinylated |
| Sugar Specificity | Sialic Acid |
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.
Maackia amurensis lectin II (MAH) is a glycoprotein consisting of two subunits each of which is composed of disulfide-linked chains.
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.
Geisler, C and Jarvis, D.L. Glycobiology, vol. 21, no. 8 pp. 988-993, 2011
Inhibitor: Human glycophorin
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