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| Alternative Names | Tau PFFs, Tau PFF, Tau protein Pre-formed Fibrils, Tau aggregates, microtubule-associated protein Tau, MAPT, MAP, microtubule-associated protein, Paired Helical Filament-Tau, Phf-Tau, Neurofibrillary Tangle Protein, G Protein Beta1/Gamma2 Subunit-Interacting Factor 1, Isoform 4, tubulin-associated unit, mouse Tau protein, P301S mutant Tau, 2N4R Tau, Tau441, fluorescent Tau fibrils, ATTO 488 conjugated 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: Cytoplasm | Axolemma | Axolemma Plasma Membrane | Axon | Cell Body | Cell membrane | 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-441 (2N4R) P301S Mutant PFFs: ATTO 488
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 hyperphosphorylated tau fibrils (3). There are six isoforms of tau in the adult human brain: three with four repeat units (4R) and three with three repeat units (3R) (4). 2N4R, or Tau-441 is the full length tau protein. P301S is a mutation encoded by exon 10 (4) that impairs the ability of tau to assemble microtubules (5).
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): Cytoplasm | Axolemma | Axolemma Plasma Membrane | Axon | Cell Body | Cell membrane | 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
- Purity: >95%
- Expression system: E. coli
- Purification: Ion-exchange Purified
- Storage buffer: PBS pH7.4, 0.09% Azide
- 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 best results, sonicate immediately prior to use. Refer to the Neurodegenerative Protein Handling Instructions on our website, or the product datasheet for further information. Monomer source is catalog# SPR-327.
Certificate of Analysis: Thioflavin T emission curve shows increased fluorescence (correlated to tau protein fibrillation) when active tau PFFs:ATTO-488 are combined with active tau monomers. Passed sterility test (OD600 equivlaent to negative control (dH20) after 139 hr incubation at 37C, 200 rpm in rich medium)
Tariff Code: 3822.19.0030
UNSPSC Code: 12352202
ADR Code: Non-hazardous
UN Code for transport: Non-hazardous
Cite this Product: Human Recombinant Tau-441 (2N4R) P301S Mutant Pre-formed Fibrils: ATTO 488 (StressMarq Biosciences | Victoria, BC CANADA | Catalog# SPR-329B-A488)
Human Recombinant Tau-441 (2N4R) P301S Mutant Pre-formed Fibrils: ATTO 488 (StressMarq Biosciences | Victoria, BC CANADA | Catalog# SPR-329C-A488)
Human Recombinant Tau-441 (2N4R) P301S Mutant Pre-formed Fibrils: ATTO 488 (StressMarq Biosciences | Victoria, BC CANADA | Catalog# SPR-329E-A488)
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How should Tau-441 (2N4R) P301S Mutant Pre-formed Fibrils: ATTO 488 (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. Alzheimer, A. Über eine eigenartige Erkrankung der Hirnrinde. Allg. Z. Psychiatr. Psych.-Gerichtl. Med. 64, 146–148 (1907)
3. Matsumoto, G. et al. (2018). Int J Mol Sci. 19, 1497.
4. Goedert, M. and Spillantini, M. G. (2017). Mol Brain. 10:18.
5. Bugiani, O. et al. (1999). J Neuropathol Exp Neurol. 58(6):667-77.