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Fig. 8 | Acta Neuropathologica Communications

Fig. 8

From: Differential effects of familial Alzheimer’s disease-causing mutations on amyloid precursor protein (APP) trafficking, proteolytic conversion, and synaptogenic activity

Fig. 8

Analysis of Aβ proteoforms in APP WT and APP FAD mutants by immunoprecipitation-mass spectrometry. IP-MALDI-TOF on A human CSF positive control, B conditioned media from wild type HEK293T cells and transiently transfected HEK293T cells with C Swedish, D Iberian, E Iowa, F Flemish and G Arctic mutations yielded mass spectra of Aβ proteoforms. Data from only one biological replicate (out of two) are shown. ¤ indicates [Aβ1-40 + 2H]2+ and * represent peaks with unknown identities. Peak identity is considered confirmed when the m/z corresponds to the theoretical m/z of an Aβ proteoforms with a tolerance of 20 ppm. In the inserts, the arrows point to the monoisotopic peak of some interesting proteoforms

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