Lentil lectin (Lens culinaris) is a metalloprotein that binds reversibly to polysaccharides and glycoconjugates containing α-D-mannose and α-D-glucose, eluting with Me-α-Man plus Me-α-Glc. Compared to Con A, it shows less discrimination between glucosyl and mannosyl residues and binds simple sugars less strongly. It retains its sugar-binding ability in the presence of 1% sodium deoxycholate, allowing it to react with detergent-solubilized membranes. Affinity-purified Lens culinaris lectin (LCA) consists of four subunits: an α-chain (MW: 5.7 kDa) and a β-chain (MW: 17.5 kDa). This lectin is useful in affinity chromatography columns for separating glycoconjugates. The two isomers, LCA-A and LCA-B, agglutinate human red blood cells without blood group specificity. The activity of LCA is assessed through hemagglutination, effectively agglutinating a 2% suspension of human erythrocytes at a concentration of 8 µg/ml. LCA requires calcium and manganese ions for binding.

Recommended Usage: Recommended dilutions of 0.5 – 20 μg/ml in Tris Buffer [Tris-HCl 0.02 M, pH 7.5] containing 1 mM CaCl₂ and 0.5 mM MnCl₂, 50 mM NaCl. 50-200 µg/ml will agglutinate type O human erythrocytes. 2-5 µg/ml will agglutinate neuraminidase treated cells.

Storage Instruction: To prevent degradation and avoid repeated freeze-thaw cycles, aliquot your product into small, single-use volumes and store them at -20°C

Application

Immunohistochemistry, Immunocytochemistry, Immunoassays, Bioconjugation, Cell typing, Neuroanatomy (tracer), Mitogen stimulator. Glycobiology.

References

1.HARVEY J. SAGE 1 and ROBERT W. GREEN. Common Lentil (Lens culinaris) Phytohemagglutinin. P 32-38. 1969. U.S. Public Health Service. Supported by NIH Grant AI-06710.
2.Michael J. Hayman and M. J . Crumpton. ISOLATION OF GLYCOPROTEINS FROM PIG LYMPHOCYTE PLASMA MEMBRANE USING Lens culinaris PHYTOHEMAGGLUTININ. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS. Vol. 47, No. 4,1972.
3.Howard IK, Sage HJ, Stein MD, Young NM, Leon MA, Dyckes DF. Studies on a phytohemagglutinin from the lentil. II. Multiple forms of Lens culinaris hemagglutinin. J Biol Chem. 1971 Mar 25;246(6):1590-5.
4.Foriers A, Lebrun E, Van Rapenbusch R, de Neve R, Strosberg AD. The structure of the lentil (Lens culinaris) lectin. Amino acid sequence determination and prediction of the secondary structure. J Biol Chem. 1981 Jun 10;256(11):5550-60.