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. 2018 Jul 23;8:11045. doi: 10.1038/s41598-018-29396-5

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© The Author(s) 2018

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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Identification of FGF21 interacting sites on β-Klotho by solid-phase binding assay. (A,B) Binding of β-Klotho in WT CM to (A) FGF21 and (B) 39F7, an anti-β-Klotho antibody, measured by solid-phase binding assay. Results are normalized to the response at the highest concentration of the biotinylated proteins. The curves and EC₅₀ values are mean ± SD of at least 3 independent experiments performed in duplicates. (C,D) EC₅₀ values determined from the solid-phase binding assay between β-Klotho and FGF21 for (C) alanine and (D) arginine mutants. EC₅₀ values are expressed as fold change relative to WT CM. *Binding curve did not converge.