Tau dGAE (297-391) Monomers

Human Recombinant Tau dGAE (297-391) Monomers

Product Specifications

Background

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) . Utilizing Tau filaments with the correct disease-specific fold is an important goal towards better mimicking specific human diseases in cellular and in vivo models. Recent Cryo-EM studies have demonstrated that recombinantly generated Tau dGAE monomers will form the disease-isolated AD or CTE Tau filament folds under highly specific conditions in vitro (4, 5) . StressMarq’s SPR-501 Tau (297-391) dGAE monomers are purified following these exact published procedures and can be utilized to form these distinct folds using specific aggregation conditions.

Product Name Alternative

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

UNSPSC

12352202

UN Code

Non-hazardous

Hazard Statement

Non-hazardous

Swiss Prot

P10636-8

Expression System

E. coli

Host

E. coli

Origin Species

Human

Target

Tau dGAE (AA297-391)

Conjugation

No Tag

Nature

Recombinant

Sequence

IKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIETHKLTFRENAKAKTDHGAE

Applications

WB | In vivo Assay | In vitro Assay

Field of Research

Purification Method

Ion-exchange, ammonium sulfate precipitation and SEC purified

Purification

Ion-exchange, ammonium sulfate precipitation and SEC purified

Limit Of Detection

Protein certified >95% pure on SDS-PAGE & Nanodrop analysis. Low endotoxin <5 EU/mL @ 2mg/mL.

Concentration

2 mg/ml or 5 mg/ml

Purity

>95%

Weight

0.02

Length

Fragment of full length wild-type Tau 2N4R (297 - 391aa)

Buffer

10mM PB pH 7.4, 10mM DTT

Molecular Weight

10.165 kDa

Precautions

Not for use in humans. Not for use in diagnostics or therapeutics. For research use only.

Additionnal Information

For corresponding PFFs, see catalog# SPR-502

References & Citations

1. Goedert, Eisenberg and Crowther. 2017. Propagation of Tau Aggregates and Neurodegeneration. Annu Rev Neurosci. DOI: https://doi.org/10.1146/annurev-neuro-072116-031153 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