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. 2018 Jan 29;10:10. doi: 10.1186/s13195-018-0337-3

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© The Author(s). 2018

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 — Molecular integrity and Alzheimer’s disease (AD) pathology: recognition of the CaptureSelect-purified GW-23B7 infused into old triple-transgenic mice. a Immunoblot showing protein stain with μ and kappa reactivity around the 1000 kDa position of an intact pentameric immunoglobulin M kappa chain (IgMκ) (lane 1). b Immunoblot of paired helical filaments (PHFs) and PHF protein kinase A purified from a human AD brain (lanes A and B) detected using a PHF-1 commercial antibody specific for hyperphosphorylated tau or using GW-23B7. Right panel shows immunohistochemical recognition by GW-23B7 of intra- and extracellular pathology-associated structures on a human AD brain section. c Immunoblots comparing reactivity to Aβ_1–42 peptide and Aβ_1–42 oligomerized (lanes C and D) by the commercial anti-Aβ 4G8/6E10 antibodies or GW-23B7; right panel shows colocalization on a human AD brain section of punctuated or strong precipitated material recognized by GW-23B7 (black stain) within amyloid plaques of Aβ detected by 4G8/6E10-specific antibodies (red stain)