Isolation of low-n amyloid β-protein oligomers from cultured cells, CSF, and brain.
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.
Center for Neurologic Diseases, Brigham & Women's Hospital, Harvard Medical School, Boston, MA, USA.
Ganesh M
GM
Shankar
Alfred T
AT
Welzel
Jessica M
JM
McDonald
Dennis J
DJ
Selkoe
Dominic M
DM
Walsh
D016229:Amyloid beta-Peptides / Q000134:cerebrospinal fluid* / Q000302:isolation & purification*; D015153:Blotting, Western; D001921:Brain / Q000378:metabolism*; D002460:Cell Line; D002478:Cells, Cultured; D002850:Chromatography, Gel; D017077:Culture Media, Conditioned / Q000737:chemistry; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D047468:Immunoprecipitation; D066298:In Vitro Techniques
D016229:Amyloid beta-Peptides; D017077:Culture Media, Conditioned