Thioflavin X (ThX)

Novel, next generation blue-green, cell-permeable fluorescent amyloid stain. Shows 5x increase in brightness and 7x increase in binding affinity to amyloidogenic proteins (α-syn) to display superior photophysical and binding properties compared to Thioflavin T (ThT). Thioflavin X (ThX) outperforms Thioflavin T as a single-aggregate probe of β-Amyloid Peptide (1-42) (human) and P301S tau as ThX is able to detect greater numbers of fluorescent species of each than ThT.

Unlike Thioflavin T, Thioflavin X (ThX) can be used for monitoring structural changes of amyloid β oligomers. The improved optical properties (extinction coefficient, quantum yield and brightness) of Thioflavin X (ThX) allow monitoring of structural differences in oligomeric species which is not observable with Thioflavin T imaging. It is suitable for studying unique structural amyloid features in bulk and on a single-aggregate level and also allows detection of amyloid β-sheet species at the early stages of protein aggregation. Also used to super-resolve the structures of tau aggregates (especially early aggregate species with lengths under 100-200 nm). Suitable for use in super-resolution microscopy with ~20nm resolution.

β-Amyloid Peptide (1-42) (human) also available.

Next generation, cell-permeable fluorescent amyloid stain with superior photophysical properties compared to Thioflavin T