English
Tau dGAE (297-391) Monomers
Human Recombinant Tau dGAE (AA297-391) Monomers
Artikelnummer
STRSPR-501XG
Verpackungseinheit
500 ug x2 (@5mg/ml)
Hersteller
Stressmarq Biosciences
Verfügbarkeit:
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Target: Tau dGAE (AA297-391)
Nature: Recombinant
Swiss-Prot: P10636-8
Expression System: E. coli
Protein Length: Fragment of full length wild-type Tau 2N4R (297 - 391aa)
Amino Acid Sequence: IKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIETHKLTFRENAKAKTDHGAE
Purification: Ion-exchange, ammonium sulfate precipitation and SEC purified
Purity: >95%
Storage Buffer: 10mM PB pH 7.4, 10mM DTT
Protein Size: 10.165 kDa
Conjugate: No Tag
Scientific Background: Filamentous 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 SPR-501 Tau (297-391) dGAE monomers are purified following these exact published procedures and can be utilized to form these distinct folds using specific aggregation conditions.
References: 1. Goedert, Eisenberg and Crowther. 2017. Propagation of Tau Aggregates and Neurodegeneration. Annu Rev Neurosci. DOI: https://doi.org/10.1146/annurev-neuro-072116-0311532. Fitzpatrick et al. 2017. Cryo-EM structures of tau filaments from Alzheimer’s disease. Nature. DOI: 10.1038/nature230023. Falcon et al. 2019. Novel tau filament fold in chronic traumatic encephalopathy encloses hydrophobic molecules. Nature. DOI: https://doi.org/10.1038/s41586-019-1026-5.4. Lovestam et al. 2022. Assembly of Recombinant Tau into Filaments Identical to those of Alzheimer’s disease and Chronic Traumatic Encephalopathy. eLife. DOI: https://doi.org/10.7554/eLife.764945. Lovestam et al. 2023. Disease-specific Tau Filaments Assemble via Polymorphic Intermediates. bioRxiv. https://doi.org/10.1101/2023.07.24.550295
Field of Use: Not for use in humans. Not for use in diagnostics or therapeutics. For research use only.
Nature: Recombinant
Swiss-Prot: P10636-8
Expression System: E. coli
Protein Length: Fragment of full length wild-type Tau 2N4R (297 - 391aa)
Amino Acid Sequence: IKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIETHKLTFRENAKAKTDHGAE
Purification: Ion-exchange, ammonium sulfate precipitation and SEC purified
Purity: >95%
Storage Buffer: 10mM PB pH 7.4, 10mM DTT
Protein Size: 10.165 kDa
Conjugate: No Tag
Scientific Background: Filamentous 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 SPR-501 Tau (297-391) dGAE monomers are purified following these exact published procedures and can be utilized to form these distinct folds using specific aggregation conditions.
References: 1. Goedert, Eisenberg and Crowther. 2017. Propagation of Tau Aggregates and Neurodegeneration. Annu Rev Neurosci. DOI: https://doi.org/10.1146/annurev-neuro-072116-0311532. Fitzpatrick et al. 2017. Cryo-EM structures of tau filaments from Alzheimer’s disease. Nature. DOI: 10.1038/nature230023. Falcon et al. 2019. Novel tau filament fold in chronic traumatic encephalopathy encloses hydrophobic molecules. Nature. DOI: https://doi.org/10.1038/s41586-019-1026-5.4. Lovestam et al. 2022. Assembly of Recombinant Tau into Filaments Identical to those of Alzheimer’s disease and Chronic Traumatic Encephalopathy. eLife. DOI: https://doi.org/10.7554/eLife.764945. Lovestam et al. 2023. Disease-specific Tau Filaments Assemble via Polymorphic Intermediates. bioRxiv. https://doi.org/10.1101/2023.07.24.550295
Field of Use: Not for use in humans. Not for use in diagnostics or therapeutics. For research use only.
Immer für Sie da
Gernot Ensinger, M.Sc.
Laurent Haze
