Amino acid residues 226-240 of tau, which encompass the first Lys-Ser-Pro site of tau, are partially phosphorylated in Alzheimer paired helical filament-tau.

@article{Liu1994AminoAR,
  title={Amino acid residues 226-240 of tau, which encompass the first Lys-Ser-Pro site of tau, are partially phosphorylated in Alzheimer paired helical filament-tau.},
  author={Wei Liu and Dennis W. Dickson and S. H. Yen},
  journal={Journal of neurochemistry},
  year={1994},
  volume={62 3},
  pages={
          1055-61
        }
}
A synthetic peptide corresponding to residues 226-240 (E9 peptide) of human tau, which contains an Lys-Ser-Pro motif, was used to raise a polyclonal antibody. The antibody, E9, was 10-fold less reactive with phospho-E9 peptide than with native E9 peptide. E9 antibody was used to study the extent of phosphorylation in a modified form of tau (PHF-tau) that is found in Alzheimer's disease brain and is incorporated into paired helical filaments (PHFs). E9 immunolabeled Alzheimer's disease… CONTINUE READING