Tau dGAE (297-391) AD-mimic Pre-formed Fibrils

Filamentous tau inclusions are a hallmark of many neurodegenerative diseases, including Alzheimer’s disease (AD) and Chronic Traumatic Encephalopathy (CTE), collectively called tauopathies. Advances in Cryo-EM have revealed that tau filaments isolated from individuals with a particular neurodegenerative disease share a distinct tau fold – i.e. an AD-isolated Tau filaments’ fold is distinct from a CTE-isolated Tau filaments’ fold (1-3) . Utilizing Tau filaments with the correct disease-specific fold is an important goal towards better mimicking specific human diseases in cellular and in vivo models. Recent Cryo-EM studies have demonstrated that recombinantly generated Tau dGAE monomers will form the disease-isolated AD or CTE Tau filament folds under highly specific conditions in vitro (4, 5) . StressMarq’s catalog# SPR-502 Tau dGAE (297-391) AD-mimic PFFs are purified and fibrilized under these exact published conditions that replicate the disease-isolated AD-fold (200 rpm at 37oC in 10 mM PB 10 mM DTT pH 7.4 200 mM MgCl2 for 48 hours) .

Tau aggregate, Tau PFFs, Tau PFF, Tau protein aggregate, Tau protein, microtubule-associated protein Tau, MAPT, MAP, microtubule-associated protein, Truncated Tau Protein Aggregate, Paired Helical Filament-Tau, Phf-Tau, Neurofibrillary Tangle Protein, dGAE Tau Protein, Tau dGAE

Alzheimer's Disease | Axon Markers | Cell Markers | Cell Signaling | Cytoskeleton | Microtubules | MT Associated Proteins | Neurodegeneration | Neuron Markers | Neuroscience | Tangles & Tau

For best results, sonicate immediately prior to use. Refer to the Neurodegenerative Protein Handling Instructions on our website, or the product datasheet for further information. Monomer source is catalog# SPR-501.

1. Goedert, Eisenberg and Crowther. 2017. Propagation of Tau Aggregates and Neurodegeneration. Annu Rev Neurosci. DOI: https://doi.org/10.1146/annurev-neuro-072116-031153 2. Fitzpatrick et al. 2017. Cryo-EM structures of tau filaments from Alzheimer’s disease. Nature. DOI: 10.1038/nature23002 3. Falcon et al. 2019. Novel tau filament fold in chronic traumatic encephalopathy encloses hydrophobic molecules. Nature. DOI: https://doi.org/10.1038/s41586-019-1026-5. 4. Lovestam et al. 2022. Assembly of Recombinant Tau into Filaments Identical to those of Alzheimer’s disease and Chronic Traumatic Encephalopathy. eLife. DOI: https://doi.org/10.7554/eLife.76494 5. Lovestam et al. 2023. Disease-specific Tau Filaments Assemble via Polymorphic Intermediates. bioRxiv. https://doi.org/10.1101/2023.07.24.550295

For best results, sonicate immediately prior to use. Refer to the Neurodegenerative Protein Handling Instructions on our website, or the product datasheet for further information. Monomer source is catalog# SPR-501.

1. Goedert, Eisenberg and Crowther. 2017. Propagation of Tau Aggregates and Neurodegeneration. Annu Rev Neurosci. DOI: https://doi.org/10.1146/annurev-neuro-072116-031153 2. Fitzpatrick et al. 2017. Cryo-EM structures of tau filaments from Alzheimer’s disease. Nature. DOI: 10.1038/nature23002 3. Falcon et al. 2019. Novel tau filament fold in chronic traumatic encephalopathy encloses hydrophobic molecules. Nature. DOI: https://doi.org/10.1038/s41586-019-1026-5. 4. Lovestam et al. 2022. Assembly of Recombinant Tau into Filaments Identical to those of Alzheimer’s disease and Chronic Traumatic Encephalopathy. eLife. DOI: https://doi.org/10.7554/eLife.76494 5. Lovestam et al. 2023. Disease-specific Tau Filaments Assemble via Polymorphic Intermediates. bioRxiv. https://doi.org/10.1101/2023.07.24.550295