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. 2023 Jun 14;13:9631. doi: 10.1038/s41598-023-36203-3

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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 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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Overview structure of PD-1 protein, cloning sequence, and SDS-PAGE result. (a) Schematic of PD-1 protein showing different domains, position of amino acid in each domain, disulfide bond location, N-linked glycosylation, predicted and identified O-linked glycosylation, range of cloning sequence, and range of purified recombinant protein with MW calculated. Amino acid positions corresponded to UniProt (Q15116). (b) SDS-PAGE analysis of recombinant PD-1 protein. Untreated (Lane 1), treated with PNGase F (Lane 2), treated with PNGase F and sialidases (Lane 3), treated with sialidases and O-protease (Lane 4), and treated with the 3 enzymes (Lane 5). Band a–e are described in text; bands correspond to PNGase F, sialidases, and O-protease enzymes are indicated. Band a* corresponds to PD-1 protein treated with sialidases and O-protease. The gel was scanned using an EPSON Expression 11000XL scanner, and images were exported using SilverFast 8.0 software. The original uncropped image of gel in this figure is provided in supplementary Fig. S1.