Generation and characterization of a rabbit monoclonal antibody site-specific for tau O-GlcNAcylated at serine 400

FEBS Lett. 2013 Nov 15;587(22):3722-8. doi: 10.1016/j.febslet.2013.09.042. Epub 2013 Oct 7.

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.

Keywords: Monoclonal antibody; O-GlcNAc; OGA; Site-specific; Tau.

MeSH terms

  • Acetylglucosamine / metabolism
  • Animals
  • Antibodies, Monoclonal / chemistry*
  • Antibody Specificity
  • Glycosylation
  • HEK293 Cells
  • Humans
  • Mice
  • Mice, Knockout
  • Protein Binding
  • Protein Processing, Post-Translational*
  • Rabbits
  • Serine / metabolism
  • tau Proteins / chemistry
  • tau Proteins / immunology*
  • tau Proteins / metabolism

Substances

  • Antibodies, Monoclonal
  • tau Proteins
  • Serine
  • Acetylglucosamine