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. 2016 Jan 22;9:36. doi: 10.1186/s13104-016-1843-7

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© Pinheiro et al. 2016

Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided 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 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.

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Fig. 4 — Analysis of purified rsccaIL-12L produced in the baculovirus-insect cell system by SDS–PAGE and Western blot. Recombinant sccaIL-12L was produced by High-five cells infected with the AcBacΔCC-sccaIL-12opt baculovirus construct at MOI 5 for 48 h. Clarified and buffer-exchanged cell culture supernatant was applied to Ni-Sepharose affinity chromatography column and the recombinant protein was eluted using an imidazole linear gradient. The chromatographic fractions were analyzed by SDS–PAGE and Western blot. Polyacrylamide gel showing: molecular weight markers (lane 1), clarified buffer-exchanged cell culture supernatant applied to the chromatographic column (10 μL, lane 2), flow through fraction (10 μL, lane 3), and sample of a chromatographic fraction containing rsccaIL-12 (10 μL, lane 4) (a). Nitrocellulose membrane showing purified sccaIL-12 incubated with normal mouse serum diluted 1:500 (lane 1) or mouse anti-his C-Term antibodies (lane 2), followed by anti-mouse immunoglobulin-alkaline phosphatase conjugate and substrate (b)