| Product Name | Tau-441 (2N4R) P301S Mutant Pre-formed Fibrils | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Description |
Human Recombinant Tau-441 (2N4R) P301S Mutant PFFs |
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| Applications | WB, SDS-PAGE, In vivo assay, In vitro assay | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Concentration | 2 mg/mL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Conjugates |
No tag
StreptavidinProperties:
Biotin
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| Nature | Recombinant | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Species | Human | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Expression System | E. coli | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Amino Acid Sequence | MAEPRQEFEV MEDHAGTYGL GDRKDQGGYT MHQDQEGDTD AGLKESPLQT PTEDGSEEPG SETSDAKSTP TAEDVTAPLV DEGAPGKQAA AQPHTEIPEG TTAEEAGIGD TPSLEDEAAG HVTQARMVSK SKDGTGSDDK KAKGADGKTK IATPRGAAPP GQKGQANATR IPAKTPPAPK TPPSSGEPPK SGDRSGYSSP GSPGTPGSRS RTPSLPTPPT REPKKVAVVR TPPKSPSSAK SRLQTAPVPM PDLKNVKSKI GSTENLKHQP GGGKVQIINK KLDLSNVQSK CGSKDNIKHVSGGGSVQIVY KPVDLSKVTS KCGSLGNIHH KPGGGQVEVK SEKLDFKDRV QSKIGSLDNI THVPGGGNKK IETHKLTFRE NAKAKTDHGA EIVYKSPVVS GDTSPRHLSN VSSTGSIDMV DSPQLATLAD EVSASLAKQG L | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Purity | >95% | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Other Resources | Sonication Protocol | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Protein Length | Full Length | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Protein Size | ~45.8 kDa | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Biological Activity | Thioflavin T emission curve shows increased fluorescence (correlated to tau protein fibrillation) when active tau PFFs are combined with active tau monomers. | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Field of Use | Not for use in humans. Not for use in diagnostics or therapeutics. For in vitro research use only. | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Storage Buffer | 10 mM HEPES, 100 mM NaCl pH 7.4 |
| Storage Temperature | -80ºC |
| Shipping Temperature | Dry Ice. Shipping note: Product will be shipped separately from other products purchased in the same order. |
| Purification | Ion-exchange Purified |
| Cite This Product | Human Recombinant Tau-441 (2N4R) P301S Mutant Pre-formed Fibrils (StressMarq Biosciences | Victoria, BC CANADA | Catalog# SPR-329) |
| Certificate of Analysis | Certified >95% pure using SDS-PAGE analysis. Low endotoxin <5 EU/mL @ 2mg/mL. |
| Other Relevant Information | 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-327. |
| Alternative Names | Tau-441, Tau-F, Tau 441, 2N4R, MAPT, TAU, MTBT1, MTBT2, MAPTL, PPND, PPP1R103, FTDP-17, PHF-Tau, Paired Helical Filament-Tau, Neurofibrillary Tangle, NFTs, intracellular neurofibrillary tangles, Tau aggregates, Tau inclusions, G Protein Beta1/Gamma2 Subunit-Interacting Factor 1, Tau PFFs |
| Research Areas | Alzheimer's Disease, Axon Markers, Cell Markers, Cell Signaling, Cytoskeleton, Microtubules, MT Associated Proteins, Neurodegeneration, Neuron Markers, Neuroscience, Tangles & Tau |
| Cellular Localization | Axolemma, Axolemma Plasma Membrane, Axon, Cell Body, Cell membrane, Cytoplasm, Cytoplasmic Ribonucleoprotein Granule, Cytoplasmic Side, Cytoskeleton, Cytosol, Dendrite, Growth cone, Microtubule, Microtubule Associated Complex, Neurofibrillary Tangle, Neuronal Cell Body, Nuclear Periphery, Nuclear Speck, Nucleus, Peripheral membrane protein, Plasma Membrane, Tubulin Complex |
| Accession Number | NP_005901.2 |
| Gene ID | 4137 |
| Swiss Prot | P10636 |
| Scientific Background |
Tau-441, the longest isoform of the microtubule-associated protein tau (MAPT), contains two N-terminal inserts and four microtubule-binding repeats (2N4R). This isoform plays a vital role in stabilizing microtubules and maintaining neuronal architecture. The P301S mutation, a proline-to-serine substitution at residue 301, is linked to familial tauopathies and significantly enhances tau’s aggregation propensity. Pre-formed fibrils (PFFs) generated from Tau-441 P301S mutant proteins replicate the structural and pathological features of tau aggregates found in neurodegenerative diseases such as frontotemporal dementia and Alzheimer’s disease. These fibrils act as potent seeds, inducing the misfolding and aggregation of endogenous tau in a prion-like manner. This seeding mechanism drives the spread of tau pathology across neural circuits, leading to synaptic dysfunction, neuroinflammation, and progressive neuronal loss. Experimental models employing P301S mutant PFFs have demonstrated their ability to initiate early tau pathology, including the formation of neurofibrillary tangles and tau-positive inclusions. These models are instrumental in dissecting the molecular mechanisms of tau propagation and identifying therapeutic targets. Tau-441 P301S mutant PFFs are essential tools for studying the dynamics of tau aggregation and its role in neurodegeneration. Their use in preclinical research accelerates the development of disease-modifying therapies aimed at halting tau spread, enhancing clearance, and restoring neuronal function in tauopathies. |
| References |
1. www.alz.org/alzheimers-dementia/facts-figures 2. Alzheimer, A. Über eine eigenartige Erkrankung der Hirnrinde. Allg. Z. Psychiatr. Psych.-Gerichtl. Med. 64, 146–148 (1907) 3. Matsumoto, G. et al. (2018). Int J Mol Sci. 19, 1497. 4. Goedert, M. and Spillantini, M. G. (2017). Mol Brain. 10:18. 5. Bugiani, O. et al. (1999). J Neuropathol Exp Neurol. 58(6):667-77. |
Thioflavin T is a fluorescent dye that binds to beta sheet-rich structures such as those in tau fibrils. Upon binding, the emission spectrum of the dye experiences a red-shift, and increased fluorescence intensity. Thioflavin T emission curves show increased fluorescence (correlated to tau aggregation) when tau Pre-formed fibrils (SPR-329) are combined with tau monomers (SPR-327). The Pre-formed fibrils seed the formation of new fibrils from a pool of monomers. Thioflavin T ex = 450 nm, em = 485 nm. 10 uM heparin was added to each well.
StressMarq Biosciences :
Based on validation through cited publications.