Abstract
Recent data suggest that soluble, non-fibrillar assemblies of the amyloid β-protein (Aβ) may mediate the synaptic deficits that characterize the early stages of Alzheimer’s disease. Consequently, much effort has been expended in isolating and studying a variety of different Aβ assemblies. Here, we describe the use of immunoprecipitation/western blotting and size exclusion chromatography/western blotting to characterize Aβ present in conditioned medium from cultured cells, human cerebrospinal fluid, and human cortex extracted with aqueous buffer, detergent, and formic acid.
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Acknowledgments
This work was supported by grants from the Wellcome Trust (067660; DMW), European Union Framework Programme 7 (200611; DMW) and the National Institutes of Health (AG027443; DJS and DMW).
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Shankar, G.M., Welzel, A.T., McDonald, J.M., Selkoe, D.J., Walsh, D.M. (2010). Isolation of Low-n Amyloid β-Protein Oligomers from Cultured Cells, CSF, and Brain. In: Roberson, E. (eds) Alzheimer's Disease and Frontotemporal Dementia. Methods in Molecular Biology, vol 670. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-60761-744-0_3
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DOI: https://doi.org/10.1007/978-1-60761-744-0_3
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