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Vector Laboratories is closed for the President’s Day on Monday, February 19th. We will be back in the office on Tuesday, February 20th.
We will respond to emails upon our return. Have a wonderful day.
Galanthus nivalis lectin, unlike most mannose-specific lectins, is not a metalloprotein and does not require Ca++ or Mn++ for binding. Binding seems to be preferentially directed toward structures containing (α-1,3) mannose residues.
| Unit Size | 5 mg |
|---|---|
| Applications | Immunohistochemistry / Immunocytochemistry, Immunofluorescence, Blotting Applications, Glycobiology |
| Recommended Usage | Although many buffers can be employed for reconstituting and diluting this lectin, 10 mM HEPES buffered saline, pH 8.5, 0.1 mM CaCl2 is recommended. Lectin may be preserved with 0.04% sodium azide. |
| Recommended Storage | 2-8 °C |
| Conjugate | Unconjugated |
| Sugar Specificity | Mannose |
In contrast to most mannose-binding lectins, GNL will not bind α-linked glucose. Reports indicate that this lectin binds rat and mouse IgM but not IgG. The only protein from human serum reported to bind to this lectin is α2-macroglobulin. GNL binds to many viral glycoproteins.
Inhibiting/Eluting Sugar: 100 mM – 200 mM α-methylmannoside
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