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Tau dGAE (297-391) C322A Mutant Monomers

Human Recombinant Tau dGAE (297-391) C322A Mutant Monomers

Product Specifications

Background

Alzheimer’s Disease (AD) is the most common neurodegenerative disease, affecting 10% of seniors over the age of 65 (1) . It was named after Alois Alzheimer, a German scientist who discovered tangled bundles of fibrils where neurons had once been in the brain of a deceased patient in 1907 (2) . 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) . A truncated 95-amino acid fragment corresponding to residues 297-391 of full-length tau has been shown to assemble into PHF-like fibrils in vitro in the absence of additives or templates (3) . This fragment has been found in the core of PHFs from AD brains and forms filaments that closely resemble PHFs isolated from AD brains (3) . The C322A mutation leads to enhanced self-assembly into long and ordered PHFs (3) .

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, G Protein Beta1/Gamma2 Subunit-Interacting Factor 1, Isoform 2, tubulin-associated unit, 95-amino acid Tau protein fragment, Truncated Tau Protein

UNSPSC

12352202

UN Code

Non-hazardous

Hazard Statement

Non-hazardous

Gene ID

4137

Swiss Prot

P10636

Accession Number

NP_005901.2

Cellular Locus

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

Expression System

E. coli

Host

E. coli

Origin Species

Human

Target

Truncated Tau Fragment (AA297-391) (dGAE)

Conjugation

No tag

Nature

Recombinant

Applications

WB | SDS-PAGE | In vivo assay | In vitro assay

Field of Research

Alzheimer's Disease | Axon Markers | Cell Markers | Cell Signaling | Cytoskeleton | Microtubules | MT Associated Proteins | Neurodegeneration | Neuron Markers | Neuroscience | Tangles & Tau

Purification Method

Ion-exchange Purified

Purification

Ion-exchange Purified

Limit Of Detection

Certified >95% pure using SDS-PAGE analysis.

Concentration

2 mg/ml

Purity

>95%

Activity

Thioflavin T emission curves show increased fluorescence (correlated to tau aggregation) over time when truncated tau fragment (AA297-391) (dGAE C322A) monomer is combined with truncated tau fragment (AA297-391) (dGAE C322A) pre-formed fibrils (Type 1) .

Weight

0.2

Length

Fragment

Buffer

PBS pH 7.4

Molecular Weight

10.133 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-461

References & Citations

1. www.alz.org/alzheimers-dementia/facts-figures 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)

Shipping Conditions

Dry Ice. Shipping note: Product will be shipped separately from other products purchased in the same order.

Storage Conditions

-80ºC

Notes

For corresponding PFFs, see catalog# SPR-461

Protein Length

Fragment

Background Reference 01

1. www.alz.org/alzheimers-dementia/facts-figures 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)

Location

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

AA Sequence

MIKHVPGGGSV QIVYKPVDLS KVTSKAGSLG NIHHKPGGGQ VEVKSEKLDF KDRVQSKIGS LDNITHVPGG GNKKIETHKL TFRENAKAKT DHGAE

Immunogen Species

Human

Curated Selection

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