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| Alternative Names | Tau 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, G Protein Beta1/Gamma2 Subunit-Interacting Factor 1, Isoform 2, tubulin-associated unit, 95-amino acid Tau protein fragment, Truncated Tau |
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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; native localization: Axolemma | Axolemma Plasma Membrane | Axon | Cell Body | Cell membrane | Cytoplasm | Cytoplasmic Ribonucleoprotein Granule | Cytoplasmic Side | Cytoskeleton | Cytosol | Dendrite | Growth cone | Microtubule | Microtubule Associated Complex | Neurofibrillary Tangle | Neuronal Cell Body | Nuclear Periphery | Nuclear Speck | Nucleus | Peripheral membrane protein | Plasma Membrane | Tubulin complex).
Human Recombinant Tau-352 (fetal 0N3R) Wild-Type Monomers
Alzheimer’s Disease (AD) is the most common neurodegenerative disease, affecting 10% of seniors over the age of 65 (1). Tau (tubulin-associated unit) is normally located in the axons of neurons where it stabilizes microtubules. Tauopathies such as AD are characterized by neurofibrillary tangles containing paired helical filaments (PHFs). Brain-specific tau isoforms vary in the number of N-terminal inserts and C- terminal repeat domains due to alternative splicing of exons; only the shortest isoform of tau, 0N3R, is expressed in the fetal brain during neurogenesis (2). Three-repeat (3R) isoforms have been shown to be more prone than four-repeat (4R) isoforms to form oligomers in vitro (3). The β-sheet core of Tau 0N3R fibrilized using heparin differs from all other tau fibril structures known to date (4).
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
- Cellular localization (native): Axolemma | Axolemma Plasma Membrane | Axon | Cell Body | Cell membrane | Cytoplasm | Cytoplasmic Ribonucleoprotein Granule | Cytoplasmic Side | Cytoskeleton | Cytosol | Dendrite | Growth cone | Microtubule | Microtubule Associated Complex | Neurofibrillary Tangle | Neuronal Cell Body | Nuclear Periphery | Nuclear Speck | Nucleus | Peripheral membrane protein | Plasma Membrane | Tubulin complex
- Protein length: Full Length (1-352 aa)
- Protein size: 37 kDa
- Purity: >95%
- Expression system: E. coli
- Purification: Ion-exchange Purified
- Storage buffer: 10 mM Hepes pH 7.4, 100 mM NaCl
- Affinity tag (sequence-indicated): GST-tag
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 Purified. Purification method and formulation help determine sample homogeneity and background in downstream biochemical assays.
Tagging: The provided sequence suggests a GST-tag, which can simplify capture/immobilization workflows in binding assays. Tag status can also influence complex formation in some contexts.
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-491
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-352 (fetal 0N3R) Wild-Type Monomers (StressMarq Biosciences | Victoria, BC CANADA | Catalog# SPR-490B)
Human Recombinant Tau-352 (fetal 0N3R) Wild-Type Monomers (StressMarq Biosciences | Victoria, BC CANADA | Catalog# SPR-490C)
Human Recombinant Tau-352 (fetal 0N3R) Wild-Type Monomers (StressMarq Biosciences | Victoria, BC CANADA | Catalog# SPR-490E)
Human Recombinant Tau-352 (fetal 0N3R) Wild-Type Monomers (StressMarq Biosciences | Victoria, BC CANADA | Catalog# SPR-490XE)
What is the purity of Tau-352 (fetal 0N3R) Wild-Type Monomers (Human)?
How should Tau-352 (fetal 0N3R) Wild-Type Monomers (Human) be stored?
What expression system was used to produce this protein?
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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. Goedert et al. Multiple isoforms of human microtubule-associated protein tau: Sequences and localization in neurofibrilary tangles of Alzheimer’s disease. Neuron. 1989;3(4):519-526.
3. Shahpasand-Kroner et al. Three-repeat and four-repeat tau isoforms for different oligomers. Prot. Sci. 2021;doi: 10.1002/pro4257
4. Dregni, et al. Inclusion of the C‑Terminal Domain in the β‑Sheet Core of Heparin-Fibrillized Three-Repeat Tau Protein Revealed by Solid-State Nuclear Magnetic Resonance Spectroscopy. JACS. 2021. https://doi.org/10.1021/jacs.1c03314