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. 2021 Feb 3;11:2854. doi: 10.1038/s41598-021-82499-4

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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 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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Immunoblots with peptide antibodies. (A) Recombinant PfM1AAP was probed with antibodies prepared against 14-mer peptides derived from the N-terminal extension (PepA), spanning domain 1 (PepB) and domain 4 (PepC) (see Supplementary Fig. 1). Anti-PfM1AAP was used as a positive control. Anti-PepA does not react with rPfM1AAP, as this lacks the N-terminal extention, whereas both anti-PepB and anti-PepC do. Lane 1 was loaded with chemilluminescent molecular marker. Lanes 2–5 were loaded with 0.25 µg of recombinant M1. (B) Cytosolic fractions of malaria parasites prepared without (−) and with (+) a protease inhibitor cocktail were probed with anti-PepA, anti-PepB and anti-PepC antibodies. Extracts were separated on 4–15% SDS-PAGE gels and transferred to nitrocellulose membrane. Lanes 2 and 3 were probed with anti-PepA, lanes 4 and 5 with anti-PepB and lanes 6 and 7 with anti-PepC antibodies. The chemiluminescent molecular marker is shown in lane 1.