Isolation of low-n amyloid β-protein oligomers from cultured cells, CSF, and brain

Methods Mol Biol. 2011;670:33-44. doi: 10.1007/978-1-60761-744-0_3.

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amyloid beta-Peptides / cerebrospinal fluid*
  • Amyloid beta-Peptides / isolation & purification*
  • Blotting, Western
  • Brain / metabolism*
  • Cell Line
  • Cells, Cultured
  • Chromatography, Gel
  • Culture Media, Conditioned / chemistry
  • Electrophoresis, Polyacrylamide Gel
  • Humans
  • Immunoprecipitation
  • In Vitro Techniques

Substances

  • Amyloid beta-Peptides
  • Culture Media, Conditioned