Ficolins constitute a group of lectins involved in innate immunity. L-Ficolin, H-ficolin, and M-ficolin are present in human serum. The human ficolins differ in carbohydrate-binding specificity, but they have in common the ability to recognize the acetyl group. L-Ficolin and H-ficolin are associated with serine proteases termed MASPs (MBL-associated serine proteases) and their truncated proteins, and the complexes (L/H-ficolin-MASP) activate the lectin pathway of complement upon binding to their ligands. Recombinant M-ficolin is also able to form a complex with MASP, resulting in complement activation. L-Ficolin and H-ficolin can be purified as a complex with MASP from serum by utilizing their binding specificities. These ficolin-MASP complexes have an ability to activate C4. Human ficolins are quantified by ELISA using specific antibodies or ligands. © 2014 Springer Science+Business Media, New York.
CITATION STYLE
Matsushita, M., Kilpatrick, D., Shiraki, H., Liu, Y., Tateishi, K., Tsujimura, M., … Fujita, T. (2014). Purification, measurement of concentration, and functional complement assay of human ficolins. Methods in Molecular Biology, 1100, 141–159. https://doi.org/10.1007/978-1-62703-724-2_12
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