Tau (K18) P301L Mutant Pre-formed Fibrils

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

Product Specifications

Background

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.

Product Name Alternative

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

UNSPSC

12352202

UN Code

Non-hazardous

Hazard Statement

Non-hazardous

Swiss Prot

P10636

Expression System

E. coli

Conjugation

No Tag

Nature

Recombinant

Applications

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

Field of Research

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

Purification

Ion-exchange Purified

Limit Of Detection

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

Concentration

2 mg/ml

Purity

> 95%

Buffer

10mM HEPES pH 7.4, 100mM NaCl

Molecular Weight

15.2 kDa

Precautions

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

Shipping Conditions

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

Storage Conditions

-80ºC

Notes

Monomer source is SPR-328

Protein Length

141 amino acids

Background Reference 01

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