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Tau-352 (fetal 0N3R) Wild-Type Monomers

Human Recombinant Tau-352 (fetal 0N3R) Wild-Type Monomers

Product Specifications

Background

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 paired helical filaments (PHFs) . Brain-specific tau isoforms vary in the number of N-terminal inserts and C- terminal repeat domains due to alternative splicing of exons; only the shortest isoform of tau, 0N3R, is expressed in the fetal brain during neurogenesis (2) . Three-repeat (3R) isoforms have been shown to be more prone than four-repeat (4R) isoforms to form oligomers in vitro (3) . The β-sheet core of Tau 0N3R fibrilized using heparin differs from all other tau fibril structures known to date (4) .

Product Name Alternative

Tau aggregate, Tau protein, microtubule-associated protein Tau, MAPT, MAP, microtubule-associated protein, Truncated Tau Protein Aggregate, 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

UNSPSC

12352202

UN Code

Non-hazardous

Hazard Statement

Non-hazardous

Gene ID

4137

Swiss Prot

P10636-2

Accession Number

NP_058525.1

Cellular Locus

Axolemma | Axolemma Plasma Membrane | Axon | Cell Body | Cell membrane | Cytoplasm | 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

Tau-352 (fetal 0N3R)

Conjugation

No Tag

Nature

Recombinant

Sequence

MAEPRQEFEVMEDHAGTYGLGDRKDQGGYTMHQDQEGDTDAGLKAEEAGIGDTPSLEDEAAGHVTQARMVSKSKDGTGSDDKKAKGADGKTKIATPRGAAPPGQKGQANATRIPAKTPPAPKTPPSSGEPPKSGDRSGYSSPGSPGTPGSRSRTPSLPTPPTREPKKVAVVRTPPKSPSSAKSRLQTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMVDSPQLATLADEVSASLAKQGL

Applications

WB | SDS-PAGE | 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

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

Full Length (1-352 aa)

Buffer

10 mM Hepes pH 7.4, 100 mM NaCl

Molecular Weight

37 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-491

References & Citations

1. www.alz.org/alzheimers-dementia/facts-figures 2. Goedert et al. Multiple isoforms of human microtubule-associated protein tau: Sequences and localization in neurofibrilary tangles of Alzheimer’s disease. Neuron. 1989;3(4):519-526. 3. Shahpasand-Kroner et al. Three-repeat and four-repeat tau isoforms for different oligomers. Prot. Sci. 2021;doi: 10.1002/pro4257 4. Dregni, et al. Inclusion of the C‑Terminal Domain in the β‑Sheet Core of Heparin-Fibrillized Three-Repeat Tau Protein Revealed by Solid-State Nuclear Magnetic Resonance Spectroscopy. JACS. 2021. https://doi.org/10.1021/jacs.1c03314

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-491

Protein Length

Full Length (1-352 aa)

Background Reference 01

1. www.alz.org/alzheimers-dementia/facts-figures 2. Goedert et al. Multiple isoforms of human microtubule-associated protein tau: Sequences and localization in neurofibrilary tangles of Alzheimer’s disease. Neuron. 1989;3 (4) :519-526. 3. Shahpasand-Kroner et al. Three-repeat and four-repeat tau isoforms for different oligomers. Prot. Sci. 2021; doi: 10.1002/pro4257 4. Dregni, et al. Inclusion of the C‑Terminal Domain in the β‑Sheet Core of Heparin-Fibrillized Three-Repeat Tau Protein Revealed by Solid-State Nuclear Magnetic Resonance Spectroscopy. JACS. 2021. https://doi.org/10.1021/jacs.1c03314

Location

Axolemma | Axolemma Plasma Membrane | Axon | Cell Body | Cell membrane | Cytoplasm | 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

MAEPRQEFEVMEDHAGTYGLGDRKDQGGYTMHQDQEGDTDAGLKAEEAGIGDTPSLEDEAAGHVTQARMVSKSKDGTGSDDKKAKGADGKTKIATPRGAAPPGQKGQANATRIPAKTPPAPKTPPSSGEPPKSGDRSGYSSPGSPGTPGSRSRTPSLPTPPTREPKKVAVVRTPPKSPSSAKSRLQTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMVDSPQLATLADEVSASLAKQGL

Immunogen Species

Human

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