Affinity purified Lens culinaris lectin (LCA) is composed of four subunits that consists of an α-chain (MW: 5.7 kDa) and β-chain (MW: 17.5 kDa). It has a carbohydrate specificity toward α-D-mannose and α-D-glucose, eluting with the sugar MeαMan+MeαGlc. This lectin is useful in affinity chromatography columns for the separation of glycoconjugates. The two isomers LCA-A and LCA-B agglutinates human red blood cells, although not blood group specific. Activity of LCA is determined by haemagglutination with human blood and agglutinates a 2% suspension of human erythrocytes at a lectin concentration of 8µg/ml. LCA requires calcium and manganese ions for binding. See other LCA conjugates.
Cy5, when bound to Lens culinaris (Lentil) Lectin (LCA/LCH), can show the binding pattern of this lectin in cellular imaging and flow cytometry. The excitation wavelength required for Cy5 to fluoresce is high enough to avoid overlap with most other fluorochromes, making it useful for dual-labeling experiments. Because of this high excitation, there is typically less background from autofluorescence of biological specimens.