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. 2022 Nov 19;23:316. doi: 10.1186/s12931-022-02240-1

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© The Author(s) 2022

Open AccessThis 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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 3 — Construction of the trivalent bispecific IL-5-HSA Nb. A The binding activity of HSA Nb towards human albumin and cynomolgus monkey albumin (CSA) at pH 5.5 and pH 7.4 was determined by ELISA. B The structure of trivalent bispecific IL-5-HSA Nb. C-D The affinity of trivalent IL-5-HSA Nb and Nucala analogue to IL-5 was detected by Fortebio