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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. 6 — Large-scale production of the trivalent IL-5-HSA Nb and its preliminary developability analysis. A The protein expression of the trivalent IL-5-HSA Nb was detected through SDS-PAGE, followed by affinity chromatography, hydrophobic chromatography and molecular sieve chromatography. The cropping gel of purified trivalent IL-5-HSA Nb is displayed. B The protein titer and wet cell weight in the fermentation tank were both measured at the indicated times. C The purity of the trivalent IL-5-HSA Nb was determined through SEC-HPLC analysis. D The stability of the trivalent IL-5-HSA Nb under different temperatures and 3 freeze‒thaw cycles was detected by SEC-HPLC and CEX-HPLC