Product Description
| Cat Number | SPR-501C |
|---|---|
| Category | Recombinant Protein |
| Pack Size | 100 µg x2 |
| Description | Human Recombinant Tau dGAE (AA297-391) Monomers |
| Applications | WB | In vivo Assay | In vitro Assay |
| Target | Tau dGAE (AA297-391) |
| Molecular Weight | 10.165 kDa |
| Purity | >95% |
| Research Area | Alzheimer's Disease | Axon Markers | Cell Markers | Cell Signaling | Cytoskeleton | Microtubules | MT Associated Proteins | Neurodegeneration | Neuron Markers | Neuroscience | Tangles & Tau |
| Swiss Prot | P10636-8 |
| Scientific Background | 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 SPR-501 Tau (297-391) dGAE monomers are purified following these exact published procedures and can be utilized to form these distinct folds using specific aggregation conditions. |
| Expression System | E. coli |
| Protein Length | Fragment of full length wild-type Tau 2N4R (297 - 391aa) |
| Amino Acid Sequence | IKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIETHKLTFRENAKAKTDHGAE |
| Purification | Ion-exchange, ammonium sulfate precipitation and SEC purified |
| Storage | -80ºC |
| References | 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 |
| Product Url | View Document |
| Note | The product is for research use only |
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