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. 2015 Jan 8;10:2. doi: 10.1186/1750-1326-10-2

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© Cuchillo-Ibañez et al.; licensee BioMed Central. 2015

This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. 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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Soluble full-length APP (sAPPf) is present in human CSF. (A) Schematic representation of full-length APP processing by α/γ-secretase (non-amyloidogenic pathway) and β/γ-secretase (amyloidogenic pathway) and the generation of extracellular large sAPPα, sAPPβ fragments, and the shorter Aβ and p3 peptides; as well as fragments containing the C-terminal APP (CTF and ICD) (not drawn in scale). The epitopes for the anti-APP antibodies used in this study are indicated. (B) Western blotting of human CSF samples from non-demented controls (NDC) subjects, resolved with the indicated anti-APP antibodies. (C, D) CSF aliquots (Total, T) were immunoprecipitated with either the anti-C-terminal APP antibody from Sigma (C, Sigma-Ct) or the pan-specific IBL-β antibody (D, IBL-β). Precipitated proteins (bound fraction, B) were immunoblotted with the antibodies as indicated. In the absence of capture-antibody (IPc), no bands were observed.