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. 2022 May 19;12:8433. doi: 10.1038/s41598-022-12423-x

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© This is a U.S. Government work and not under copyright protection in the US; foreign copyright protection may apply 2022

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 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/.

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Increased levels of CAP256V2LS tyrosine sulfation correspond to increased antigen binding. (a) Octet antigen-binding curve for fractions of CAP256V2LS generated from CHO clone 206. (b) Relative antigen binding potency (%RP) for each level of tyrosine sulfation proteoform of CAP256V2LS. Octet antigen-binding curve for fractions of (c) CHO clone 386 and (d) CAP256V2LS expressed in HEK-293 cells. %RPs were normalized against the highest 4-SO₃ proteoform from the same parent material. Binding curve data points shown as average with error bars are from two independently prepared experiments.