Generation and characterization of a rabbit monoclonal antibody site-specific for tau O-GlcNAcylated at serine 400 |
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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 |
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| Institution: | 1. EMD Serono Research & Development Institute, Billerica, MA 01821, United States;2. Asceneuron SA, Lausanne, Switzerland;3. McLaughlin Research Institute, Great Falls, MT 59405, United States |
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| 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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| Keywords: | O-GlcNAc Tau Site-specific Monoclonal antibody OGA |
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