Monoclonal antibody PHF-9 recognizes phosphorylated serine 404 of tau protein and labels paired helical filaments

✍ Scribed by Frank P. Zemlan; Gary E. Dean

• Book ID: 102653368
• Publisher: John Wiley and Sons
• Year: 1996
• Tongue: English
• Weight: 775 KB
• Volume: 46
• Category: Article
• ISSN: 0360-4012
• DOI: 10.1002/(sici)1097-4547(19961001)46:1<90::aid-jnr11>3.0.co;2-g

✦ Synopsis

Paired helical filaments (PHFs) purified from Alzheimer's brain consist of hyperphosphorylated microtubule-associated protein tau. In PHF, phosphorylation occurs at ser/thr tau residues. Several of these ser/thr phosphorylation sites lie immediately C-terminal to the tau tubulin binding domain. The C-terminal ser396 to thr4I3 tau region contains two or more phosphorylated residues and eight possible ser/thr phosphorylation sites. Immunologic studies and mass spectroscopy have identified ser396 as one of the phosphorylation sites but identification of more C-terminal phosphorylated residues has been hampered by the lack of monoclonal antibodies (Mabs) that recognize defined epitopes in this region.