DESCRIPTION

• Nature: Recombinant
• Purity: >95%
• Target: Tau-352 (fetal 0N3R)
• Category: Protein
• Conjugate: No Tag
• References: 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
• Applications: WB | SDS-PAGE | In vitro Assay
• Field of Use: Not for use in humans. Not for use in diagnostics or therapeutics. For research use only.
• Protein Size: 37 kDa
• Purification: Ion-exchange Purified
• Concentration: Lot/batch specific. See included datasheet.
• Protein Length: Full Length (1-352 aa)
• Research Areas: Alzheimer's Disease | Axon Markers | Cell Markers | Cell Signaling | Cytoskeleton | Microtubules | MT Associated Proteins | Neurodegeneration | Neuron Markers | Neuroscience | Tangles & Tau
• Storage Buffer: 10 mM Hepes pH 7.4, 100 mM NaCl
• Alternative Names: 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
• Cite This Product: Human Recombinant Tau352 (fetal 0N3R) Pre-formed Fibrils (StressMarq Biosciences Inc., Victoria BC CANADA, Catalog # SPR-491)
• Expression System: E. coli
• Species Full Name: Human
• Amino Acid Sequence: MAEPRQEFEVMEDHAGTYGLGDRKDQGGYTMHQDQEGDTDAGLKAEEAGIGDTPSLEDEAAGHVTQARMVSKSKDGTGSDDKKAKGADGKTKIATPRGAAPPGQKGQANATRIPAKTPPAPKTPPSSGEPPKSGDRSGYSSPGSPGTPGSRSRTPSLPTPPTREPKKVAVVRTPPKSPSSAKSRLQTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMVDSPQLATLADEVSASLAKQGL
• Storage Temperature: -80ºC
• Shipping Temperature: Dry Ice. Shipping note: Product will be shipped separately from other products purchased in the same order.
• Cellular Localization: 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
• Scientific 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).
• Certificate of Analysis: Protein certified >95% pure on SDS-PAGE & Nanodrop analysis