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P2–044: Inducible cell models of tauopathy show that tau aggregation is toxic to cells, but tau pathology can be reversed
Author(s) -
Biernat Jacek,
Khlistunova Inna,
Wang Yipeng,
Pickhardt Marcus,
Gazova Zuzana,
Mandelkow Eva Maria
Publication year - 2006
Publication title -
alzheimer's and dementia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 6.713
H-Index - 118
eISSN - 1552-5279
pISSN - 1552-5260
DOI - 10.1016/j.jalz.2006.05.881
Subject(s) - tauopathy , neurodegeneration , mutant , tau protein , protein aggregation , chemistry , phosphorylation , microbiology and biotechnology , biology , biophysics , biochemistry , alzheimer's disease , medicine , disease , gene
antibody (detection). 2) Taking advantage of an APP construct containing an N-terminal secreted alkaline phosphatase (SEAP) domain, we have also developed a convenient hybrid ELISA-SEAP assay. This assay utilizes the -site-specific antibody to capture SEAP-tagged sAPP in cell culture media, followed by alkaline phosphatase substrate metabolism for easy colorimetric detection. Conclusions: These methods offer valuable tools to develop a new and potential biomarker of AD and to discover therapeutic agents that target the -cleavage of APP in cell-based assays.