| Species : |
Galanthus nivalis |
| Source : |
Galanthus nivalis |
| Tag : |
Non |
| Description : |
Galanthus nivalis lectin, unlike most mannose-specific lectins, is not a metalloprotein and does not require Ca2+ or Mn2+ for binding. Binding seems to be preferentially directed toward structures containing (α-1,3) mannose residues. Also 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. |
| Bio-activity : |
Inhibiting/Eluting Sugar: 100 mM - 200 mM α-methylmannoside |
| Molecular Mass : |
50 kDa |
| Applications : |
Immunohistochemistry / Immunocytochemistry, Immunofluorescence, Blotting Applications, Glycobiology |
| Storage : |
Refrigerate at 4 centigrade |
| Reconstitution : |
Although many buffers can be employed for reconstituting and diluting this lectin, 10 mM HEPES buffered saline, pH 8.5, 0.1 mM Ca2+ is recommended. Lectin may be preserved with 0.04% sodium azide. |
