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.
Accompanying each fluorescent lectin is an analysis data sheet summarizing the results of our quality control tests and providing pertinent information on the product. All of these reagents are supplied as solutions perserved with sodium azide.
Fluorescein labeled LCA has an appropriate number of fluorochromes bound to provide the optimum staining characteristics for this lectin. This conjugate is supplied essentially free of unconjugated fluorochromes. The excitation maximum is at 495 nm and the emission maximum is at 515 nm.
Inhibiting/Eluting Sugar: mixture of 200 mM α-methylmannoside/200 mM α-methylglucoside