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. 2020 Oct 13;6:70. doi: 10.1038/s41421-020-00201-w

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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 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. 6 — a E. coli-expressed MBP-tagged WT-CARD^aa1–101 and VLLV-CARD^aa1–101 protein both elute as two peaks. b Multi-angle light scattering (MALS) analysis of VLLV-CARD^aa1–101 monomer peak in a. c ASTRA analysis of the molecular weight of different peaks in b. d Gel-filtration chromatography of truncated CARDs with the same quantity of proteins (1 mg). e Gel-filtration chromatography analysis of MBP-tagged WT-CARD^aa1–101 and VLLV-CARD^aa1–101 with a GS repeat sequence. f CARD inhibition of p30 proteolytic activity was detected by the fluorescence derived from the GSDMD cleavage reporter. CARD(1) indicates the concentration ratio between the catalytic domain and CARD protein as 1 : 1; CARD(2) indicates 1 : 2; CARD(3) indicates 1 : 3.