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. 2021 Aug 28;9:146. doi: 10.1186/s40478-021-01242-2

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© The Author(s) 2021

Open AccessThis 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/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 7 — Biochemical fractionation followed by immunoblotting demonstrating that αSyn carboxy truncated at residue 125 is abundant in the brain of LBD patients. LBD temporal cortex adjacent to the amygdala, LBD amygdala (*), and control temporal cortex adjacent to the amygdala were biochemically fractionated as described in “Material and Methods”. 20 ug of protein from the soluble (high salt soluble) and insoluble (SDS/urea) fractions were analyzed by immunoblotting with antibody 3H11 with epitope in the middle of αSyn residues 43–62 and antibody 5C1 specific for αSyn carboxy truncated at residue 125. The relative mobilities of molecular mass protein markers are identified on the left of the blots. Arrow indicates full-length αSyn and asterisk truncated αSyn