重組人 Tau dGAE (297-391) 模擬AD前體原纖維 (無肝素輔助聚集) Catalog No. SPR-502。如需購買Stressmarq公司產(chǎn)品，請聯(lián)系Stressmarq全國總代理欣博盛生物。

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Alternative NamesTau aggregate, Tau PFFs, Tau PFF, Tau protein aggregate, Tau protein, microtubule-associated protein Tau, MAPT, MAP, microtubule-associated protein, Truncated Tau Protein Aggregate, Paired Helical Filament-Tau, Phf-Tau, Neurofibrillary Tangle Protein, dGAE Tau Protein, Tau dGAEResearch AreasMT 相關(guān)蛋白, 神經(jīng)元標記物, 神經(jīng)纖維纏結(jié)&Tau, 神經(jīng)退行性疾病, 細胞標記物, 軸突標記物, 微管, 神經(jīng)生物學, 阿爾茨海默病, 細胞信號傳導(dǎo), 細胞骨架Swiss ProtP10636-8Scientific BackgroundFilamentous tau inclusions are a hallmark of many neurodegenerative diseases, including Alzheimer’s disease (AD) and Chronic Traumatic Encephalopathy (CTE), collectively called tauopathies. Advances in Cryo-EM have revealed that tau filaments isolated from individuals with a particular neurodegenerative disease share a distinct tau fold – i.e. an AD-isolated Tau filaments’ fold is distinct from a CTE-isolated Tau filaments’ fold (1-3). Utilizing Tau filaments with the correct disease-specific fold is an important goal towards better mimicking specific human diseases in cellular and in vivo models. Recent Cryo-EM studies have demonstrated that recombinantly generated Tau dGAE monomers will form the disease-isolated AD or CTE Tau filament folds under highly specific conditions in vitro (4, 5). StressMarq’s catalog# SPR-502 Tau dGAE (297-391) AD-mimic PFFs are purified and fibrilized under these exact published conditions that replicate the disease-isolated AD-fold (200 rpm at 37oC in 10 mM PB 10 mM DTT pH 7.4 200 mM MgCl2 for 48 hours).References1. Goedert, Eisenberg and Crowther. 2017. Propagation of Tau Aggregates and Neurodegeneration. Annu Rev Neurosci. 
2. Fitzpatrick et al. 2017. Cryo-EM structures of tau filaments from Alzheimer’s disease. Nature. 
3. Falcon et al. 2019. Novel tau filament fold in chronic traumatic encephalopathy encloses hydrophobic molecules. Nature. 
4. Lovestam et al. 2022. Assembly of Recombinant Tau into Filaments Identical to those of Alzheimer’s disease and Chronic Traumatic Encephalopathy. eLife. 
5. Lovestam et al. 2023. Disease-specific Tau Filaments Assemble via Polymorphic Intermediates. bioRxiv. 

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