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Tau Truncated Fragment (AA297-391) (dGAE C322A) Monomers
Human Recombinant Truncated Tau Fragment (AA297-391) (dGAE C322A) Protein Monomers
Artikelnummer
STRSPR-445B
Verpackungseinheit
100 µg
Hersteller
Stressmarq Biosciences
Verfügbarkeit:
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Target: Tau.
Nature: Recombinant.
Swiss-Prot: P10636.
Biological 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) preformed fibrils (Type 1).
Expression System: E. coli.
Protein Length: Fragment .
Purification: Ion-exchange Purified.
Purity: >95%.
Storage Buffer: PBS pH 7.4.
Protein Size: 10.133 kDa.
Conjugate: No tag.
Cellular Localization: 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.
Scientific 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).
References: 1. www.alz.org/alzheimers-dementia/facts-figures2. 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).
Field of Use: Not for use in humans. Not for use in diagnostics or therapeutics. For research use only.
Nature: Recombinant.
Swiss-Prot: P10636.
Biological 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) preformed fibrils (Type 1).
Expression System: E. coli.
Protein Length: Fragment .
Purification: Ion-exchange Purified.
Purity: >95%.
Storage Buffer: PBS pH 7.4.
Protein Size: 10.133 kDa.
Conjugate: No tag.
Cellular Localization: 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.
Scientific 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).
References: 1. www.alz.org/alzheimers-dementia/facts-figures2. 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).
Field of Use: Not for use in humans. Not for use in diagnostics or therapeutics. For research use only.
| Artikelnummer | STRSPR-445B |
|---|---|
| Hersteller | Stressmarq Biosciences |
| Hersteller Artikelnummer | SPR-445B |
| Green Labware | Nein |
| Verpackungseinheit | 100 µg |
| Mengeneinheit | STK |
| Reaktivität | Human |
| Methode | Western Blotting, In Vivo Assay, SDS-PAGE |
| Human Gene ID | 4137 |
| Produktinformation (PDF) |
|
| MSDS (PDF) | Download |
Immer für Sie da
Gernot Ensinger, M.Sc.
Laurent Haze
