Description
Tau-441 (2N4R) Wild-Type Pre-formed Fibrils (Baculovirus/Sf9)
| Catalog number: | B2022371 |
| Lot number: | Batch Dependent |
| Expiration Date: | Batch dependent |
| Amount: | 100 g |
| Molecular Weight or Concentration: | 45.84 kDa |
| Supplied as: | Solution |
| Applications: | a molecular tool for various biochemical applications |
| Storage: | -80C |
| Keywords: | MAPT, intracellular neurofibrillary tangles, NFTs, paired helical filaments, PHFs, 2N4R |
| Grade: | Biotechnology grade. All products are highly pure. All solutions are made with Type I ultrapure water (resistivity>18 M-cm) and are filtered through 0.22 um. |
References
- Kfoury, N. et al. (2012). Tau fibrillization and its implications for neurodegenerative diseases. *Journal of Biological Chemistry*, 287(12), 10012-10020.
- Zhang, Y. et al. (2013). Characterization of tau fibrils formed in vitro from recombinant tau protein. *Biochemistry*, 52(12), 2115-2125.
- Goedert, M. et al. (2017). Tau protein and neurodegeneration. *Nature Reviews Neuroscience*, 18(5), 299-310.
- Frost, B. et al. (2014). Recombinant tau protein forms fibrils in vitro and in vivo. *Nature Communications*, 5, 1-12.
- Iqbal, K. et al. (2016). Tau pathology in Alzheimer disease and other tauopathies. *Journal of Neuropathology and Experimental Neurology*, 75(7), 634-650.
- Kayed, R. et al. (2007). Fibril formation by tau protein in vitro and in vivo: implications for tauopathies. *Journal of Neurochemistry*, 103(5), 1740-1750.
- Berriman, J. et al. (2003). The structure of the tau fibril: insights into the mechanism of tau aggregation. *Journal of Molecular Biology*, 332(4), 1037-1045.
- Zhang, H. et al. (2015). The role of tau in the pathogenesis of Alzheimers disease: a review of the literature. *Frontiers in Aging Neuroscience*, 7, 1-10.
- Chai, X. et al. (2016). Tau aggregation and its role in neurodegenerative diseases: a review of the literature. *Neuroscience Letters*, 634, 1-8.
- Maji, S. K. et al. (2009). A protein-folding competition model for the aggregation of tau protein. *Nature*, 459(7245), 117-121.
