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. 2023 Aug 31;14:5291. doi: 10.1038/s41467-023-41117-9

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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 Binding of D11 and E07 mAbs to human (h) and mouse (m) Gal-3 constructs (FL, full-length; CRD, carbohydrate recognition domain) and their selectivity towards human Gal-1 and Gal-7, measured by ELISA. Each mAb (D11, red; E07, blue) was tested at 20 µg/mL, and the appropriate positive control (commercial antibody against Gal-3, Gal-1, or Gal-7; Ctrl, gray bars) was used at 5 µg/mL. An irrelevant IgG (Irr) was used as a negative control for each assay. b Dose–response ELISA of D11 and E07 mAbs binding to hGal-3 (solid lines) and mGal-3 (dotted lines). c Dose–response competition between asialofetuin (ASF) and D11 and E07 mAbs to hGal-3. d K_D values of D11 and E07 mAbs to recombinant Gal-3 from multiple species (h, human; m, mouse; r, rat; c, cynomolgus; d, dog) by SPR. Data are representative of one experiment performed during the anti-Gal-3 IgG selection flow scheme.