tau phosphorylation assay from Innoprot allows the identification of tau kinase and phosphatase inhibitors and modulators that affect the behaviour or location of tau protein.
Tau is a group of neuronal microtubule-associated proteins that are formed by alternative mRNA splicing. They accumulate in neurofibrillary tangles in Alzheimer’s disease (AD) brain. There is significant evidence that a disruption of normal phosphorylation events results in tau dysfunction. It is a contributing factor to the pathogenic processes of neurodegenerative diseases, such as AD.
In this tau phosphorylation assay, we use a U2OS cell line stably expressing triple mutant (TM) human 0N4R Tau-tGFP. Binding of tau to microtubules and consecuent bundle-formation is phosphorylation dependent. Hyperphosporylation of tau leads to its dissociation from microtubules and aggregation into tangles of paired helical filaments (PHF). On the contrary, kinase inhibitors promote tau binding to microtubules and the formation of microtubule bundles.
Quantification of bundles by image analysis allows the identification of tau kinase and phosphatase inhibitors.