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. 2022 May 19;20:237. doi: 10.1186/s12951-022-01456-z

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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. 2 — The affinity test of anti-hANGPTL3-CCD VHHs and epitope binning assay. a Identification of ANGPTL3 specific VHHs from 48 clones specifically binding with hANGPTL3 after three rounds bio-panning. b The SDS-PAGE analysis of the C27-His6, C44-His6 and C46-His6. M: Maker; lane 1: C27-His6; lane 2: C44-His6; lane 3: C46-His6. c–e The affinity of C27-His6, C44-His6 and C46-His6 binding to hANGPTL3 (S17-P220)-His6. f The assay for hANGPTL3-binding epitopes of the C44-His6 was performed against evinacumab by the dual antibody sandwich ELISA. The horizontal and vertical axes represent the concentrations of the C44-His6 and the OD450 value