| Field | Specification |
|---|---|
| Mfr No | |
| Alternative Names | MAPT, intracellular neurofibrillary tangles, NFTs, paired helical filaments, PHFs, 2N4R |
| Concentration | |
| Conjugate | |
| Expression System | |
| Product Type | |
| Protein Length | |
| Protein Size | |
| Purity | |
| Shipping | |
| Species | |
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| Target |
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-441 (2N4R) P301S Mutant PFFs (CHO-expressed, N-glycosylated)
Field of Use
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 Neuroscience and Neurodegeneration.
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: 441 aa (excluding tag), 466 aa (including tag)
- Protein size: 48.609 kDa
- Purity: >95%
- Expression system: Chinese Hamster Ovary (CHO)
- Purification: Affinity Purified and Size Exclusion
- Storage buffer: 1X PB pH7.4, 2mM DTT
- Affinity tag (sequence-indicated): His-tag
Post-translational considerations: Mammalian expression can support native-like folding, disulfide bond formation, and glycosylation. These features are often important for secreted proteins, receptors, and adhesion molecules where PTMs influence binding and stability.
Expression and purification strategy
Expression system: Chinese Hamster Ovary (CHO). Expression host choice can influence folding and PTM state, which may affect binding or activity depending on protein class.
Purification strategy: Affinity Purified and Size Exclusion. Purification method and formulation help determine sample homogeneity and background in downstream biochemical assays.
Tagging: The provided sequence suggests a His-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: CHO expression in mammalian cell line may lead to more “human” like phosphorylation/glycosylation patterns. 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-515.
Certificate of Analysis: Protein certified >95% pure on SDS-PAGE & Nanodrop analysis
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 (StressMarq Biosciences | Victoria, BC CANADA | Catalog# SPR-516B)
Human Recombinant Tau-441 (2N4R) P301S Mutant Pre-formed Fibrils (StressMarq Biosciences | Victoria, BC CANADA | Catalog# SPR-516C)
Human Recombinant Tau-441 (2N4R) P301S Mutant Pre-formed Fibrils (StressMarq Biosciences | Victoria, BC CANADA | Catalog# SPR-516E)
Human Recombinant Tau-441 (2N4R) P301S Mutant Pre-formed Fibrils (StressMarq Biosciences | Victoria, BC CANADA | Catalog# SPR-516XE)
What is the purity of Tau-441 (2N4R) P301S Mutant Pre-formed Fibrils (Human)?
How should Tau-441 (2N4R) P301S Mutant Pre-formed Fibrils (Human) be stored?
What expression system was used to produce this protein?
What are the shipping conditions?
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. Losev et al., 2020. Differential effects of putative N-glycosylation sites in human Tau on Alzheimer’s disease-related neurodegeneration. Cellular and Molecular Life Sciences. DOI: 10.1007/s00018-020-03643-3
3. Zhang et al., 2020. Integrative glycoproteomics reveals protein N-glycosylation aberrations and glycoproteomic network alterations in Alzheimer’s disease. Sci. Adv. DOI: 10.1126/sciadv.abc5802
4. Liu et al., 2002. Role of glycosylation in hyperphosphorylation of tau in Alzheimer’s disease. FEBS. DOI: 10.1016/S0014-5793(02)02228-7
5. Losev et al., 2019. Novel model of secreted human tau protein reveals the impact of the abnormal N-glycosylation of tau on its aggregation propensity. Sci. Rep. https://doi.org/10.1038/s41598-019-39218-x
6. Bugiani et al., 1999. Frontotemporal Dementia and Corticobasal Degeneration in a Family with a P301S Mutation in Tau. J Neuropathol Exp Neurol. doi: 10.1097/00005072-199906000-00011.
7. Goedert and Crowther, 1999. Effects of frontotemporal dementia FTDP-17 mutations on heparin-induced assembly of tau filaments. FEBS Lett. DOI: 10.1016/s0014-5793(99)00508-7