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. 2020 Nov 5;10:19122. doi: 10.1038/s41598-020-75571-y

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© The Author(s) 2020

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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Purification of Gc proteins by vitamin D affinity column chromatography. CBB staining patterns of two independently prepared samples of Gc1F, purified with His-Trap column chromatography (A, Gc1F 1 and 2) and blotting patterns with anti-Gc antibody (B, Gc1F 1 and 2). The eluate from the His-Trap column (A, Gc1F 1) was subjected to vitamin D affinity column chromatography. Affinity-purified Gc1F was detected by CBB staining (C). Gc1S and Gc2 were similarly purified and stained with CBB (D). The CBB staining pattern of mouse GcMAF purified by a single step of vitamin D affinity column chromatography (E). Full-length gels and blots are included in a Supplementary Fig. 4.