Lens culinaris agglutinin (LCA, LcH), biotinylated

Lens culinaris agglutinin is composed of four subunits - two of about 17 kDa and two of 8 kDa. 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. 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. Biotinylated Lens culinaris agglutinin 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 sodium azide. 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. Inhibiting/Eluting Sugar: mixture of 200 mM α-methylmannoside/200 mM α-methylglucoside

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