Figure S1. Artificial plaques formed through aggregation of Aβ42 peptide form beta sheet structures and can therefore serve as a model for the plaques found in the brain of patients with Alzheimer disease. The presence of beta sheet structures is shown by thioflavin T binding and subsequent emission of green fluorescence. Left column: Artificial plaques and non-aggregated Aβ peptide in agarose were stained with 3 mM thioflavin T solution and pictures were taken at excitation and emission wavelengths of 485 and 550 nm, respectively. Green fluorescence can be seen in artificial plaques, but not in Aβ42 peptide. Right column: Artificial plaque or Aβ peptide in agarose stained with monoclonal antibody NAB228 against beta-amyloid. Staining for amyloid can be seen in both peptide and artificial plaque. In the sections of the non aggregated peptide staining is evenly distributed in the agarose, whereas aggregates can be seen in the sections with the artificial plaque.

Figure S2. A. A modified antigen retrieval method, which does not cause pCRP dissociation does not affect staining for monomeric and pentameric CRP. Human brain tissue from the frontal cortex of patients with Alzheimer disease demonstrates positive staining (brown) with the antibody clones 9C9 (mCRP-specific) and NAB228 (beta-amyloid-specific), whereas almost no staining is detectable with clone 8D8 (pCRP-specific). B. Incubating pCRP in 0.1% CaCl2 at 50°C overnight does not cause dissociation into its monomeric isoform. pCRP was diluted in 0.1% CaCl2 and then incubated at 50°C for 12 h and then run on a 10% native gel followed by native Western blotting and staining with conformation-specific antibodies (clone ID6: pCRP; clone 9C9: mCRP). As a positive control for dissociation, pCRP in PBS was incubated at 95°C for 10 minutes.

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