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. 2022 Jun 20;13:3542. doi: 10.1038/s41467-022-31062-4

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© The Author(s) 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 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. 1 — A The mucinome comprises a variety of proteins that have a densely glycosylated mucin domain. Mucin domains are found in canonical mucins, mucin-domain glycoproteins, and even multi-pass transmembrane proteins. B Workflow for enrichment technique. StcE^E447D beads were conjugated using reductive amination to POROS-AL 20 beads, followed by capping in Tris-HCl (1). Complex samples (lysate, ascites) were added to the beads and allowed to bind overnight (2), washed, and eluted by boiling in protein loading buffer (3). Samples were fractionated via one-dimensional gel electrophoresis and digested in-gel using trypsin (4); the gel electrophoresis chamber was created with BioRender.com.