Recombinant full-length and truncated Factor H.

<p>(<b>A</b>) Schematic representation of fH structure that includes 20 SCR domains and design of recombinant fH molecules used in our experiments. Amino acid lengths and SCR domains of each recombinant fragment are shown. (<b>B</b>) Immunoblotting (IB) of purified recombinant full-length and truncated fH molecules using polyclonal anti-fH antibody. (<b>C</b>) Purified recombinant full-length and truncated fH molecules were detected after PAGE (10%) and Coomassie blue staining. (<b>D</b>) C3b was incubated with plasma purified and recombinant fH molecules and immunoprecipitated using polyclonal anti-C3 antibody. Precipitated proteins were immunoblotted using anti-fH antibody. (<b>E</b>) Cofactor activity of plasma purified and recombinant fH molecules was investigated by incubating them with purified C3b and factor I. Factor I-mediated cleavage of C3b generated two cleavage products (arrowheads) originated form C3b α chain.