LCA recognizes sequences containing α-linked mannose residues but recognizes additional sugars as part of the receptor structure, giving it a narrower specificity than Con A. An α-linked fucose residue attached to the N-acetylchitobiose portion of the core oligosaccharide significantly enhances affinity. By exploiting this narrower specificity, glycoproteins and glycopeptides can be subfractionated with LCA after initial isolation with Con A.
Unit Size | 10 mg, 25 mg |
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Applications | Immunohistochemistry / Immunocytochemistry, Immunofluorescence, Blotting Applications, Glycobiology, Mitogenic Stimulation |
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. For preserving solutions stored at 4 ºC, 0.08% sodium azide can be used. |
Recommended Storage | 2-8 °C |
Inhibiting and/or Eluting Sugar | mixture of 200 mM α−methylmannoside/200 mM α−methylglucoside |
Conjugate | Unconjugated |
Sugar Specificity | Mannose, Glucose |
Lens culinaris agglutinin is composed of four subunits – two of about 17 kDa and two of 8 kDa. LCA has been found to be one of the most effective agents in preventing skin allograft rejection in model systems. LCA has been used to purify numerous glycoproteins, including immunoglobulins, histocompatibility antigens, and α2-macroglobulin.
Inhibiting/Eluting Sugar: mixture of 200 mM α-methylmannoside/200 mM α-methylglucoside
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