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Home > Publication > Detection and Quantification Methods for Fibrillar Products of In Vitro Tau Aggregation Assays

Detection and Quantification Methods for Fibrillar Products of In Vitro Tau Aggregation Assays

Nanavaty N, Lin L, Hinckley S H, et al.

Tau Protein: Methods and Protocols, 2017: 101-111.

Alzheimer’s disease is characterized in part by the intracellular misfolding and aggregation of tau protein. The aggregates, which range in size from small oligomers to large flaments, are markers for disease diag nosis and staging, potential vectors for disease propagation, and candidate sources of neurotoxicity. Here, the author present protocols for synthesizing large tau aggregates characterized by flamentous morphology and cross-β-sheet structure from monomeric full-length tau precursors in vitro. The authors also describe their detection and quantifcation through thioflavin dye binding, flter trap, and transmission electron microscopy methods. These methods cover applications requiring high-throughput capability as well as those requiring high-resolution analysis of aggregation mechanism.

Chemicals Used in the Paper:

Catalog Number Product Name Structure CAS Number Price
ACM8003847 GERANINE G GERANINE G 8003-84-7 Price

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Email:
Tel:1-201-478-8534
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Fax: 1-516-927-0118
Address: 2200 Smithtown Avenue, Room 1 Ronkonkoma, NY 11779-7329 USA