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P2‐126: Stepwise proteolysis liberates tau fragments that nucleate the aggregation of tau and tau‐dependent toxicity in a neuronal cell model
Author(s) -
Wang Yipeng,
Biernat Jacek,
Pickhardt Marcus,
Mandelkow Eckhard,
Mandelkow Eva-Maria
Publication year - 2008
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.2008.05.1200
Subject(s) - proteolysis , cleavage (geology) , tau protein , chemistry , c terminus , biophysics , fragmentation (computing) , protein aggregation , mutant , in vitro , stereochemistry , biochemistry , microbiology and biotechnology , biology , alzheimer's disease , amino acid , enzyme , medicine , paleontology , ecology , disease , pathology , fracture (geology) , gene
been mostly characterized by ELISA techniques with only a few anti-PHFTau mAbs studied with Tau phosphorylated in-vitro. Here we mapped mAbs directed against the Tau230-240-region using unphosphorylated, monophosphorylated (pThr231, pSer235) and doublyphosphorylated (pThr231 pSer235) tau protein constructs which have been coupled to human aldo/keto reductase AKR1A1 by native chemical ligation and analysed by western blotting. Conclusions: The obtained epitope-specificities were very similar to the data obtained by ELISA, only one mAb showed higher cross-reactivity. Since immuno based assays gained more and more influence in the field of diagnosis and analysis. In order to establish a selective and sensitive assay, the knowledge of the epitope of the applied antibody is essential.