Competition with Aβ1-42 against the increased antibody binding found after acid dissociation of sera from APP mice vaccinated with Aβ

<p><b>Copyright information:</b></p><p>Taken from "Overcoming antigen masking of anti-amyloidbeta antibodies reveals breaking of B cell tolerance by virus-like particles in amyloidbeta immunized amyloid precursor protein transgenic mice"</p><p>BMC Neuroscience 2004;5():21-21.</p><p>Published online 8 Jun 2004</p><p>PMCID:PMC442125.</p><p>Copyright © 2004 Li et al; licensee BioMed Central Ltd. This is an Open Access article: verbatim copying and redistribution of this article are permitted in all media for any purpose, provided this notice is preserved along with the article's original URL.</p> Sera were collected from transgenic mice, diluted 1:1000 and preincubated at either pH 7 (open bars) or pH 2.5 (solid bars) as described in methods. After centrifugation and reconstitution of serum volume, the sera were incubated with Aβ1-42 at the indicated concentrations. Because the Aβ was initially dissolved in DMSO, some samples were also incubated with DMSO at the concentrations found in the 100 μg/ml Aβ incubation (2% DMSO). ELISA assays were completed as described in Methods and the optical density at 450 nm used to estimate the amount of antibody binding to the ELISA plate. Results are presented as mean ± sem