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. 2020 May 12;20:26. doi: 10.1186/s12896-020-00616-z

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© The Author(s) 2020

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. 6 — GoldenBac facilitates screening of chaperone co-expression constructs. Ten different baculoviruses expressing the TwinStrep-tagged HOIP (TS-HOIP) protein together with different combinations of chaperones were generated and HOIP expression levels were analyzed. Composition of the constructs HC1–10 are described in Table 1. a. Total cell lysates were analyzed by Western blotting to detect TS-HOIP and FLAG-tagged HSPA8, HSPA1A, sfHSPA8, or DNAJA1. The baculovirus protein gp64 was used as a loading control. b. Soluble fractions were also analyzed by Western blotting for TS-HOIP. c. SDS-PAGE analysis of the purification of TS-HOIP alone (left) or of construct HC2, which contains TS-HOIP co-expressed with HSPA8 and DNAJA1 (right). HSPA8 is visible as a contaminant in the elution