| Storage Buffer | 10mM Hepes pH 7.4, 100mM NaCl |
| 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-383 (0N4R) Wild-Type Monomers (StressMarq Biosciences | Victoria, BC CANADA | Catalog# SPR-509) |
| Certificate of Analysis | Protein certified >95% pure on SDS-PAGE & Nanodrop analysis. Low endotoxin <5 EU/mL @ 2mg/mL. |
| Other Relevant Information | For corresponding PFFs, see catalog# SPR-510 |
| Alternative Names | Tau-383, Tau-D, Microtubule-associated protein tau, MAPT, TAU, MTBT1, MTBT2, MAPTL, PPND, PPP1R103, FTDP-17, Tau-40, PHF-Tau, Paired Helical Filament-Tau, Neurofibrillary Tangle, Isoform 4, G Protein Beta1/Gamma2 Subunit-Interacting Factor 1 |
| Research Areas | Alzheimer's Disease, Neurodegeneration, Neuroscience, Tangles & Tau |
| Swiss Prot | P10636-6 |
| Scientific Background |
Tau-383, also known as the 0N4R isoform of the microtubule-associated protein tau (MAPT), is a naturally occurring variant composed of 383 amino acids. It lacks N-terminal inserts but contains all four microtubule-binding repeat domains, making it one of the most aggregation-prone tau isoforms expressed in the adult human brain. In its monomeric form, Tau-383 plays a critical role in stabilizing microtubules and supporting axonal transport. However, under pathological conditions, Tau-383 monomers can misfold and initiate self-assembly into toxic oligomers and fibrils—key events in the development of tauopathies such as Alzheimer’s disease, progressive supranuclear palsy, and corticobasal degeneration. Tau-383 wild-type monomers are widely used in neurodegenerative disease research to model early-stage tau aggregation and to investigate the molecular triggers of misfolding. Their defined structure and high aggregation propensity make them ideal for in vitro assays, structural studies, and therapeutic screening platforms. By enabling precise analysis of tau dynamics, Tau-383 monomers support the development of targeted interventions aimed at preventing aggregation, enhancing clearance, and restoring neuronal function. Their use accelerates translational research focused on halting tau-driven neurodegeneration and improving outcomes for patients with tauopathies. |
| References |
1. Goedert et al. 1989. Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer’s disease. Neuron. DOI: 10.1016/0896-6273(89)90210-9 2. Goedert, Eisenberg and Crowther. 2017. Propagation of Tau Aggregates and Neurodegeneration. Annual Review of Neuroscience. DOI: 10.1146/annurev-neuro-072116-031153 3. Dregni et al. 2022. Fluent molecular mixing of Tau isoforms in Alzheimer’s disease neurofibrillary tangles. Nature communications. DOI: 10.1038/s41467-022-30585-0 |
In vitro seeding activity of human tau-383 (0N4R) monomers in ThT assay. Full length, wild-type tau 2N4R fibrils (SPR-480) seed fibril formation of human Tau-383 (0N4R) monomers over 72 hours. Reactions (100uL) shaken at 600 rpm in Greiner-Bio 96 Well Non-Binding Cell Culture Microplates, Black (Greiner-Bio Catalog #655900) at 37oC and read with an XPS Microplate Reader set at 450nmex/485nmem.
Reviews
There are no reviews yet.