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. 2018 Jul 30;9:1586. doi: 10.3389/fimmu.2018.01586

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Copyright © 2018 Al-Ahdal, Murugaiah, Varghese, Abozaid, Saba, Al-Qahtani, Pathan, Kouser, Nal and Kishore.

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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SDS-PAGE (12% v/v) under reducing conditions showing expression and purification of a recombinant surfactant protein D (rfhSP-D). The neck and carbohydrate recognition domain regions were expressed in Escherichia coli BL21 (λDE3) pLysS. (A) Following induction with 0.5 mM IPTG, a ~20 kDa band appeared being overexpressed compared to uninduced sample. Following denaturation–renaturation cycle, the rfhSP-D was purified on an affinity column to homogeneity after elution with EDTA as fractions F1, F2 and F3 (B). A rabbit polyclonal antibody raised against full-length SP-D purified from human bronchoalveolar lavage (C) recognized the purified rfhSP-D, but not BSA that was used as a negative control protein.