Tau (K18) P301L Mutant Voorgevormde fibrillen

Tauopathies are a class of neurodegenerative diseases characterized by the pathological aggregation of tau protein. The K18 fragment, comprising the microtubule-binding repeat domains of tau, is frequently used in experimental models due to its propensity to form fibrillar aggregates. The P301L mutation, located within the repeat domain, has been demonstrated to increase the protein's propensity to aggregate and seed, making it a key variant in modeling tau pathology. Our Tau (K18) P301L Mutant Pre-formed Fibrils are fibrillized without heparin and have been demonstrated to be neurotoxic to primary mouse cortical neurons.

Human Recombinant Tau (K18) P301L Mutant Pre-Formed Fibrils (fibrillized without heparin)

Tau PFFs, Tau PFF, Tau protein Pre-formed Fibrils, Tau aggregates, microtubule-associated protein Tau, MAPT, MAP, microtubule-associated protein, Paired Helical Filament-Tau, Phf-Tau, Neurofibrillary Tangle Protein, G Protein Beta1/Gamma2 Subunit-Interacting Factor 1, Isoform 4, tubulin-associated unit

12352202

Non-hazardous

Non-hazardous

P10636

E. coli

No Tag

Recombinant

WB | SDS-PAGE | In vivo assay | In vitro assay

Neuroscience | Neurodegeneration | Alzheimer's Disease | Tangles & Tau

Ion-exchange Purified

Protein certified > 95% pure via SDS-PAGE and A260/A280 ratio

2 mg/ml

> 95%

10mM HEPES pH 7.4, 100mM NaCl

15.2 kDa

Not for use in humans. Not for use in diagnostics or therapeutics. For research use only.

Dry Ice. Shipping note: Product will be shipped separately from other products purchased in the same order.

-80ºC

Monomer source is SPR-328

141 amino acids

1. Peeraer, E., Bottelbergs, A., Van Kolen, K., Stancu, I. C., Vasconcelos, B., Mahieu, M., Duytschaever, H., Ver Donck, L., Torremans, A., Sluydts, E., Van Acker, N., Kemp, J. A., Mercken, M., Brunden, K. R., Trojanowski, J. Q., Dewachter, I., Lee, V. M., & Moechars, D. (2015) . Intracerebral injection of preformed synthetic tau fibrils initiates widespread tauopathy and neuronal loss in the brains of tau transgenic mice. Neurobiology of disease, 73, 83–95. https://doi.org/10.1016/j.nbd.2014.08.032 2. Croft, C. L., Goodwin, M. S., Ryu, D. H., Lessard, C. B., Tejeda, G., Marrero, M., Vause, A. R., Paterno, G., Cruz, P. E., Lewis, J., Giasson, B. I., & Golde, T. E. (2021) . Photodynamic studies reveal rapid formation and appreciable turnover of tau inclusions. Acta Neuropathologica, 141, 359–381. https://doi.org/10.1007/s00401-021-02264-9 3. Zhang, X., Wang, J., Zhang, Z., & Ye, K. (2024) . Tau in neurodegenerative diseases: molecular mechanisms, biomarkers, and therapeutic strategies. Translational Neurodegeneration, 13 (40) . https://doi.org/10.1186/s40035-024-00429-6

MSRLQTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVLGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIETHKLTFRE

Human