Tau-441 (2N4R) P301S Mutant Pre-formed Fibrils (CHO-expressed, N-glycosylated)
Product Sizes
100 ug
SPR-516-100UG
2 x 100 ug
SPR-516-2X100UG
500 ug
SPR-516-500UG
About this Product
- SKU:
- SPR-516
- Additional 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
- Application:
- Cell-based/Functional Assay, Western Blot
- Buffer:
- 1X PB pH7.4, 2mM DTT
- CE/IVD:
- RUO
- Extra Details:
- Tau-441, the longest isoform of the microtubule-associated protein tau (MAPT), comprises 441 amino acids and includes two N-terminal inserts and four microtubule-binding repeat domains. The P301S mutation, located within the fourth repeat domain, is a well-characterized pathogenic variant associated with frontotemporal dementia and other tauopathies. Pre-formed fibrils (PFFs) generated from Tau-441 P301S mutant monomers exhibit enhanced aggregation kinetics, structural stability, and seeding capacity compared to wild-type tau fibrils. These mutant PFFs closely mimic the pathological tau aggregates found in human neurodegenerative diseases, making them a powerful tool for modeling disease progression. In cellular and animal models, Tau-441 P301S PFFs efficiently seed endogenous tau, induce neurofibrillary tangle formation, and trigger neurodegenerative cascades including synaptic dysfunction, neuroinflammation, and neuronal loss. Their reproducibility and disease relevance support mechanistic studies of tau propagation, prion-like transmission, and isoform-specific pathology. Tau-441 P301S mutant PFFs are widely used in therapeutic screening platforms to evaluate compounds that inhibit tau aggregation, block intercellular spread, or enhance tau clearance. By replicating key features of tau-driven neurodegeneration, these fibrils accelerate translational research and drug development for Alzheimer's disease, frontotemporal dementia, and related tauopathies. Mammalian N-glycosylation is present on CHO-secreted tau 2N4R, which contributes to slower migration on SDS-PAGE than E.coli or Baculovirus/Sf9 expressed tau (1, 2). N-glycosylated tau has been identified in human AD-diseased brains, but not healthy brains, and may precede tau hyperphosphorylation (3, 4). N-glycosylation of Tau has been demonstrated to affect its aggregation propensity (5). The tau P301S mutation is associated with early onset neurodegeneration, and functionally reduces microtubule assembly and stimulates fibril assembly (6, 7). StressMarq's CHO-expressed Tau 2N4R P301S PFFs are generated in the absense of heparin and contain mammalian post-translational modifications that may better mimic tau in human AD-brains.
- Immunogen:
- Tau-441 (2N4R) P301S PFFs
- Molecular Weight:
- 48.609 kDa
- Purity:
- >95%
- Purification:
- Affinity Purified and Size Exclusion
- Sequence:
- GGSHHHHHHHHHHGSGGSENLYFQGMAEPRQEFEVMEDHAGTYGLGDRKDQGGYTMHQDQEGDTDAGLKESPLQTPTEDGSEEPGSETSDAKSTPTAEDVTAPLVDEGAPGKQAAAQPHTEIPEGTTAEEAGIGDTPSLEDEAAGHVTQARMVSKSKDGTGSDDKKAKGADGKTKIATPRGAAPPGQKGQANATRIPAKTPPAPKTPPSSGEPPKSGDRSGYSSPGSPGTPGSRSRTPSLPTPPTREPKKVAVVRTPPKSPSSAKSRLQTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVSGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMVDSPQLATLADEVSASLAKQGL
- Shipping Conditions:
- Dry Ice
- Storage Conditions:
- -70[o]C
- Supplier:
- StressMarq Biosciences
- Type:
- Proteins, Peptides, Small Molecules & Other Biomolecules: Recombinant Proteins
