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. 2019 Apr 2;10:637. doi: 10.3389/fimmu.2019.00637

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Copyright © 2019 Ju, Xu, Zhu, Fu, Morel and Xu.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Expression, purification, and detection of histone-binding affinity of the mouse sNASP protein. Proteins were expressed in E. coli and purified using ion-exchange chromatography and size exclusion chromatography. (A) The purity of recombinant WT sNASP and rec1c sNASP proteins was more than 90% as confirmed by SDS-PAGE gel. Biolayer interferometer was used to detect the affinity of WT sNASP and rec1c sNASP proteins binding mouse histones H1a, H3.1, H4, and H3.1/H4 tetramer. (B) A graph of a representative assay shows the interaction of WT sNASP binding histone 4 at the indicated concentrations from 62.5 to 1,000 nM. Each experiment is represented by an initial baseline (a), a sNASP immobilization curve (b), another baseline (c), an association curve (d), and a disassociation curve (e).