Tau oligomers have been shown to be the main toxic tau species in a number of neurodegenerative disorders. In order to study tau oligomers both in vitro and in vivo, we have established methods for the reliable preparation, isolation, and detection of tau oligomers. Methods for the seeding of tau oligomers, isolation of tau oligomers from tissue, and detection of tau oligomers using tau oligomer-specific antibodies by biochemical and immunohistochemical methods are detailed below.
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Brain-derived tau oligomer polymorphs: distinct aggregations, stability profiles, and biological activities.
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Article Synopsis
- Tau is a protein that helps maintain the structure and function of neurons, but it misfolds in diseases like Alzheimer's, leading to neuronal damage.
- Soluble tau oligomers, which are toxic to neurons, disrupt synaptic function and contribute to disease progression, making them important targets for study.
- Traditional detection methods struggle with sensitivity for small tau aggregates, but advanced techniques like smFRET and SiMPull provide better insights, aiding in earlier detection and potential therapy development for tau-related diseases.
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