Premium
Generation and characterization of a rabbit monoclonal antibody site‐specific for tau O‐GlcNAcylated at serine 400
Author(s) -
Cameron Andrew,
Giacomozzi Brandy,
Joyce John,
Gray Audrey,
Graham Danielle,
Ousson Solenne,
Neny Maud,
Beher Dirk,
Carlson George,
O'Moore Jill,
Shearman Mark,
Hering Heike
Publication year - 2013
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2013.09.042
Subject(s) - monoclonal antibody , tau pathology , tau protein , neurotoxicity , serine , in vivo , chemistry , in vitro , antibody , biophysics , biochemistry , alzheimer's disease , biology , phosphorylation , immunology , medicine , disease , toxicity , pathology , genetics , organic chemistry
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.