Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10870826 | FEBS Letters | 2013 | 7 Pages |
Abstract
Aggregation of tau into paired helical filaments is a pathological process leading to neurotoxicity in Alzheimer's disease and other tauopathies. Tau is posttranslationally modified by O-linked N-acetylglucosamine (O-GlcNAc), and increasing tau O-GlcNAcylation may protect against its aggregation. Research tools to study the relationship between tau aggregation and tau O-GlcNAcylation have not been widely available. Here we describe the generation of a rabbit monoclonal antibody specific for tau O-GlcNAcylated at Ser400 (O-tau(S400)). We show the utility of this antibody for in vitro and in vivo experiments to investigate the function of O-GlcNAc modifications of tau at Ser400.
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Authors
Andrew Cameron, Brandy Giacomozzi, John Joyce, Audrey Gray, Danielle Graham, Solenne Ousson, Maud Neny, Dirk Beher, George Carlson, Jill O'Moore, Mark Shearman, Heike Hering,