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. 2023 Jan 13;6:42. doi: 10.1038/s42003-023-04431-y

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© The Author(s) 2023

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 4 — a A concentration series of human, murine, and disulphide trapped C9 variants in the monomeric state detected by aE11 IgG in a slot immunoblot assay. An arrow shows the approximate physiological concentration of monomeric C9 (900 ± 200 nM)^59,60. b Analytical ultracentrifugation of wild type and disulphide-trapped C9 at micromolar concentration shows only monomeric C9 species. c Mass photometry measurements of the molecular mass of C9 variants corroborates AUC measurements (n = 2). Lower molecular weight peaks (~10 kDa) of R65Q and P72E variants correspond to a known contaminant. d Maximal SPR response of aE11 IgG binding versus concentration of monomeric C9 and variants (n = 2). e Maximal binding of aE11 IgG to monomeric C9 at 150 nM (n = 2). f Kinetic fit of off-rate for one-to-one binding of aE11 IgG to monomeric C9 (n = 2). Individual data points and their means are plotted.