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.
Horseradish peroxidase (HRP) is a 40 kDa protein that catalyzes the oxidation of substrates by hydrogen peroxide, resulting in a colored or fluorescent product or release of light as a byproduct of the reaction. It is most commonly used for blotting, immunoassays and immunohistochemistry methods. Lens culinaris (Lentil) Lectin (LCA/LCH) is conjugated to HRP at an appropriate ratio to provide optimal staining characteristics.