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|
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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