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. 2020 Aug 4;11:1728. doi: 10.3389/fimmu.2020.01728

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Copyright © 2020 Haque, Cortes, Alam, Sreedhar, Ferreira and Pangburn.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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SDS-PAGE of purified fragments of human Factor H. Recombinant proteins were expressed in High Five insect cells grown in serum free media. The proteins were purified from the media by ion exchange and affinity chromatography. Proteins spanning the C-terminal domains of Factor H (rH 16-20, rH 17-20, rH 18-20, and rH 19-20 with calculated molecular weights of 39, 32, 26, and 19 kDa, respectively), and standards with the indicated size were electrophoresed through 8–16% gradient polyacrylamide gels under reducing condition and stained with Coomassie blue dye. Figure is a composite of multiple gels.