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| Alternative Names | Tau monomer, Tau protein monomer, Tau protein, microtubule-associated protein Tau, MAPT, MAP, microtubule-associated protein, Truncated Tau Protein Monomer, Paired Helical Filament-Tau, Phf-Tau, Neurofibrillary Tangle Protein, Tau dGAE Protein, dGAE |
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| Expression System | |
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Background
Tau is provided as a recombinant protein reagent for research use only. It is commonly used as a defined molecular component in biochemical and cell-free systems where controlled protein input supports mechanistic study and assay development.
Protein identity context: Tau (source species: Human).
Human Recombinant Tau dGAE (297-391) Monomers
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).
Biological significance and function
Tau is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This protein is frequently discussed in research themes such as Alzheimer's Disease and Axon Markers.
Molecular characteristics
Molecular characteristics: Key molecular attributes can influence binding behavior, stability, and assay background—especially for multimeric, disulfide-rich, or PTM-dependent proteins.
- Source species: Human
- Protein length: Fragment of full length wild-type Tau 2N4R (297 - 391aa)
- Protein size: 10.165 kDa
- Purity: >95%
- Expression system: E. coli
- Purification: Ion-exchange, ammonium sulfate precipitation and SEC purified
- Storage buffer: 10mM PB pH 7.4, 10mM DTT
Post-translational considerations: E. coli expression typically yields a non-glycosylated recombinant form. This is often appropriate for intracellular enzymes and many binding studies, but extracellular ligands/receptors or disulfide-rich proteins may show activity or stability differences when PTMs are required.
Expression and purification strategy
Expression system: E. coli. Expression host choice can influence folding and PTM state, which may affect binding or activity depending on protein class.
Purification strategy: Ion-exchange, ammonium sulfate precipitation and SEC purified. Purification method and formulation help determine sample homogeneity and background in downstream biochemical assays.
Research interpretation
Research interpretation: Recombinant protein reagents can support controlled experiments such as reconstitution of molecular interactions, quantitative calibration, and mechanistic perturbation studies with defined inputs. Interpreting outcomes typically benefits from pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex formation.
Other relevant information: For corresponding PFFs, see catalog# SPR-502
Certificate of Analysis: Protein certified >95% pure on SDS-PAGE & Nanodrop analysis. Low endotoxin <5 EU/mL @ 2mg/mL.
Tariff Code: 3822.19.0030
UNSPSC Code: 12352202
ADR Code: Non-hazardous
UN Code for transport: Non-hazardous
Cite this Product: Human Recombinant Tau dGAE (297-391) Monomers (StressMarq Biosciences | Victoria, BC CANADA | Catalog# SPR-501B)
Human Recombinant Tau dGAE (297-391) Monomers (StressMarq Biosciences | Victoria, BC CANADA | Catalog# SPR-501C)
Human Recombinant Tau dGAE (297-391) Monomers (StressMarq Biosciences | Victoria, BC CANADA | Catalog# SPR-501E)
Human Recombinant Tau dGAE (297-391) Monomers (StressMarq Biosciences | Victoria, BC CANADA | Catalog# SPR-501XE)
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How should Tau dGAE (297-391) Monomers (Human) be stored?
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Is this protein approved for clinical or in vitro diagnostic use?
Can I request a custom size, tag variant, or formulation?
Can’t Find What You’re Looking For? We can help you source the best match or customize a recombinant protein solution for your study. Options may include species (human/mouse/rat), protein region/domain (full-length vs fragment), tag or label (His/GST/FLAG/biotin/fluorescent), expression system (E. coli/HEK293/insect), purity grade, formulation (buffer, carrier-free, glycerol-free), activity/functional validation (binding or enzymatic assays), endotoxin level (low-endotoxin for cell-based work), mutants/variants (point mutations, isoforms), and bulk or custom packaging. Click Talk to a Scientist to submit a request form, email us at support@biohippo.com, or explore our Research Services for additional support. Our team will be in contact with you shortly.
2. Fitzpatrick et al. 2017. Cryo-EM structures of tau filaments from Alzheimer’s disease. Nature. DOI: 10.1038/nature23002
3. 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.76494
5. Lovestam et al. 2023. Disease-specific Tau Filaments Assemble via Polymorphic Intermediates. bioRxiv. https://doi.org/10.1101/2023.07.24.550295