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Tau-441 (2N4R) P301S Mutant Monomers

Human Recombinant Tau-441 (2N4R) P301S 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 hyperphosphorylated tau fibrils (3) . There are six isoforms of tau in the adult human brain: three with four repeat units (4R) and three with three repeat units (3R) (4) . 2N4R, or Tau-441 is the full length tau protein. P301S is a mutation encoded by exon 10 (4) that impairs the ability of tau to assemble microtubules (5) .

Product Name Alternative

Tau monomer, Tau protein monomer, Tau protein, microtubule-associated protein Tau, MAPT, MAP, microtubule-associated protein, Tau-441, Paired Helical Filament-Tau, Phf-Tau, Neurofibrillary Tangle Protein, G Protein Beta1/Gamma2 Subunit-Interacting Factor 1, Isoform 2, tubulin-associated unit

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

Tau-441 (2N4R) P301S Mutant

Conjugation

No tag

Nature

Recombinant

Sequence

MAEPRQEFEV MEDHAGTYGL GDRKDQGGYT MHQDQEGDTD AGLKESPLQT PTEDGSEEPG SETSDAKSTP TAEDVTAPLV DEGAPGKQAA AQPHTEIPEG TTAEEAGIGD TPSLEDEAAG HVTQARMVSK SKDGTGSDDK KAKGADGKTK IATPRGAAPP GQKGQANATR IPAKTPPAPK TPPSSGEPPK SGDRSGYSSP GSPGTPGSRS RTPSLPTPPT REPKKVAVVR TPPKSPSSAK SRLQTAPVPM PDLKNVKSKI GSTENLKHQP GGGKVQIINK KLDLSNVQSK CGSKDNIKHVSGGGSVQIVY KPVDLSKVTS KCGSLGNIHH KPGGGQVEVK SEKLDFKDRV QSKIGSLDNI THVPGGGNKK IETHKLTFRE NAKAKTDHGA EIVYKSPVVS GDTSPRHLSN VSSTGSIDMV DSPQLATLAD EVSASLAKQG L

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. Low endotoxin <5 EU/mL @ 2mg/mL.

Concentration

2 mg/ml

Purity

>95%

Activity

Thioflavin T emission curve shows increased fluorescence (correlated to tau protein fibrillation) when tau PFFs are combined with tau monomers.

Weight

0.2

Length

Full Length

Buffer

10 mM HEPES, 100 mM NaCl pH 7.4

Molecular Weight

~45.8 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-329

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. Matsumoto, G. et al. (2018). Int J Mol Sci. 19, 1497. 4. Goedert, M. and Spillantini, M. G. (2017). Mol Brain. 10:18. 5. Bugiani, O. et al. (1999). J Neuropathol Exp Neurol. 58(6):667-77.

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-329

Protein Length

Full Length

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. Matsumoto, G. et al. (2018) . Int J Mol Sci. 19, 1497. 4. Goedert, M. and Spillantini, M. G. (2017) . Mol Brain. 10:18. 5. Bugiani, O. et al. (1999) . J Neuropathol Exp Neurol. 58 (6) :667-77.

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

MAEPRQEFEV MEDHAGTYGL GDRKDQGGYT MHQDQEGDTD AGLKESPLQT PTEDGSEEPG SETSDAKSTP TAEDVTAPLV DEGAPGKQAA AQPHTEIPEG TTAEEAGIGD TPSLEDEAAG HVTQARMVSK SKDGTGSDDK KAKGADGKTK IATPRGAAPP GQKGQANATR IPAKTPPAPK TPPSSGEPPK SGDRSGYSSP GSPGTPGSRS RTPSLPTPPT REPKKVAVVR TPPKSPSSAK SRLQTAPVPM PDLKNVKSKI GSTENLKHQP GGGKVQIINK KLDLSNVQSK CGSKDNIKHVSGGGSVQIVY KPVDLSKVTS KCGSLGNIHH KPGGGQVEVK SEKLDFKDRV QSKIGSLDNI THVPGGGNKK IETHKLTFRE NAKAKTDHGA EIVYKSPVVS GDTSPRHLSN VSSTGSIDMV DSPQLATLAD EVSASLAKQG L

Immunogen Species

Human

Curated Selection

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