| Field | Specification |
|---|---|
| Mfr No | |
| Accession Number | |
| Alternative Names | Tau, MAPT, Microtubule-associated protein tau, Microtubule associated protein tau, Microtubule associated protein tau isoform 4, TAU_HUMAN, TAU, MAPTL, MTBT1, MTBT2, RNPTAU, PHF-tau, PHF tau, Paired helical filament tau, Paired helical filament-tau, Neurofibrillary tangle protein, DDPAC, FTDP 17, MSTD, PPND, PPP1R103, Protein phosphatase 1 regulatory subunit 103, G protein beta1/gamma2 subunit interacting factor 1, AI413597, AW045860, FLJ31424, MGC134287, MGC138549, MGC156663, dGAE tau fibril, Truncated Tau Fragment (AA297-391), 95-amino acid tau protein fragment, Truncated Tau Protein |
| Cellular Localization | |
| Clonality | |
| Concentration | |
| Host | |
| Immunogen | Recombinant Human Tau AA297-391 (dGAE) Fibril (SPR-461) |
| Product Type | |
| Reactivity | |
| Shipping | |
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| Target |
Tau is a microtubule-associated protein encoded by the MAPT gene and plays a vital role in stabilizing neuronal microtubules. In Alzheimer’s disease (AD) and related tauopathies, tau undergoes pathological modifications that lead to its aggregation into paired helical filaments (PHFs), forming neurofibrillary tangles—a hallmark of AD.
A truncated tau fragment comprising residues 297–391, known as Tau dGAE, represents a minimal core region capable of self-assembling into PHF-like fibrils in vitro without the need for cofactors or templates. This 95-amino acid segment has been identified in the core of PHFs extracted from AD brain tissue and forms filaments that closely mimic those observed in human pathology.
Tau dGAE is a powerful model for studying the molecular mechanisms of tau aggregation, seeding, and propagation. Its ability to recapitulate key structural features of pathological tau makes it an essential tool for developing aggregation inhibitors, imaging agents, and immunotherapies targeting tau fibrils.
By isolating the aggregation-prone core of tau, researchers can dissect the structural transitions and biochemical interactions that drive neurodegeneration, making Tau dGAE a critical focus in Alzheimer’s disease research and therapeutic development.
A 1:1000 dilution of SPC-806 was sufficient for detection of tau in 15 μg of mouse, rat brain cell lysates by ECL immunoblot analysis using goat anti-rabbit IgG:HRP as the secondary antibody.
Cite this product varies by variant:
- SPC-806D — Size: 100 ug: Tau Antibody (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SPC-806D, RRID: AB_3716851)
- SPC-806D-A390 — Size: 100 ug: Tau Antibody: ATTO 390 (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SPC-806D-A390, RRID: AB_3716852)
- SPC-806D-A488 — Size: 100 ug: Tau Antibody: ATTO 488 (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SPC-806D-A488, RRID: AB_3716853)
- SPC-806D-A594 — Size: 100 ug: Tau Antibody: ATTO 594 (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SPC-806D-A594, RRID: AB_3716854)
- SPC-806D-APC — Size: 100 ug: Tau Antibody: APC (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SPC-806D-APC, RRID: AB_3716855)
- SPC-806D-BI — Size: 100 ug: Tau Antibody: Biotin (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SPC-806D-BI, RRID: AB_3716856)
- SPC-806D-FITC — Size: 100 ug: Tau Antibody: FITC (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SPC-806D-FITC, RRID: AB_3716857)
- SPC-806D-HRP — Size: 100 ug: Tau Antibody: HRP (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SPC-806D-HRP, RRID: AB_3716858)
- SPC-806D-PCP — Size: 100 ug: Tau Antibody: PerCP (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SPC-806D-PCP, RRID: AB_3716859)
- SPC-806D-RPE — Size: 100 ug: Tau Antibody: RPE (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SPC-806D-RPE, RRID: AB_3716860)
- SPC-806S — Size: 12 ug: Tau Antibody (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SPC-806S, RRID: AB_3716851)
Customization & Add-ons: Can’t find the antibody you need—or require a custom format for your assay? We can help you source the best match or support custom antibody solutions for diverse research needs, including species and isotype selection, conjugations and labeling (e.g., HRP/AP, biotin, fluorophores), purification grade options (Protein A/G, affinity purified), formulation preferences (buffer selection, carrier-free, glycerol-free), custom concentrations and aliquoting, low-endotoxin options for cell-based work, and application-focused QC/validation support (project dependent). Click Talk to a Scientist to submit a request, email us at support@biohippo.com, or explore our Research Services for additional support—our team will follow up with feasibility details and next steps.
2. Alzheimer, A. Über eine eigenartige Erkrankung der Hirnrinde. Allg. Z. Psychiatr. Psych.-Gerichtl. Med. 64, 146–148 (1907)
3. Al-Hilaly, Y.K. et al. Alzheimer's Disease-like Paired Helical Filament Assembly from Truncated Tau Protein Is Independent of Disulfide Crosslinking. J. Mol. Biol. 429(23):3650-3665 (2017)