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. 2016 Jun 1;13:132. doi: 10.1186/s12974-016-0591-x

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© The Author(s). 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. 1 — Schematic representation of the potential cross-reactivity of anti-Met-enkephalin and anti-β-endorphin polyclonal IgG antibodies. The amino acid sequence of Met-enkephalin (five amino acids corresponding to only one epitope, gray box) is identical to the first five amino acids of the β-endorphin and may be recognized by immune serum IgG specifically raised against Met-enkephalin () or β-endorphin ()

Inline graphic — Schematic representation of the potential cross-reactivity of anti-Met-enkephalin and anti-β-endorphin polyclonal IgG antibodies. The amino acid sequence of Met-enkephalin (five amino acids corresponding to only one epitope, gray box) is identical to the first five amino acids of the β-endorphin and may be recognized by immune serum IgG specifically raised against Met-enkephalin () or β-endorphin ()