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. 2021 Jun 24;12:3950. doi: 10.1038/s41467-021-24273-8

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© The Author(s) 2021

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 Western blot analysis of EV-enriched protein TSG101 in milk-derived EV samples. b TEM images of RM and CM EVs. c NTA revealed major peak as 145 nm for RM and 135 nm for CM samples. d Equal protein amount of EVs from RM and colorectal cancer cells (LIM1215) were acidified (pH = 2) or boiled (15 min at 105 °C), subjected to ultracentrifugation and final total volumes were assessed for stability by western blotting for EV-enriched protein TSG101. e Schematic representation of the assay to test the role of calcium in EV stability. f Equal amounts of milk-derived EVs were treated with EGTA prior to acidification or boiling. The samples were subjected to ultracentrifugation and final total volumes were assessed by Western blot analysis for TSG101 (n = 3). All data are represented as mean ± s.e.m. Statistical significance was determined by two-tailed t-test. g Venn diagram of differentially abundant proteins identified in RM and CM EVs (n = 3). h Heatmap depicting the small RNA profile of RM and CM EVs (R-biological replicate) (n = 3).