{"product_id":"tau-dgae-297-391-monomers-bhp11901141","title":"Tau dGAE (297-391) Monomers","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eTau\u003c\/strong\u003e is provided as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. It is commonly used as a defined molecular component in biochemical and cell-free systems where controlled protein input supports mechanistic study and assay development.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eProtein identity context:\u003c\/strong\u003e Tau (source species: Human; native 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).\u003c\/p\u003e\u003cp\u003eHuman Recombinant Tau dGAE (297-391) Monomers\u003c\/p\u003e\u003cp\u003eAlzheimer’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). 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).\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eTau\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This protein is frequently discussed in research themes such as \u003cstrong\u003eAlzheimer's Disease\u003c\/strong\u003e and \u003cstrong\u003eAxon Markers\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Key molecular attributes can influence binding behavior, stability, and assay background—especially for multimeric, disulfide-rich, or PTM-dependent proteins.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eCellular localization (native):\u003c\/strong\u003e 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\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e Fragment\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein size:\u003c\/strong\u003e 10.165 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt;95%\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurification:\u003c\/strong\u003e Ion-exchange Purified\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eStorage buffer:\u003c\/strong\u003e PB pH 7.4\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often appropriate for intracellular enzymes and many binding studies, but extracellular ligands\/receptors or disulfide-rich proteins may show activity or stability differences when PTMs are required.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression host choice can influence folding and PTM state, which may affect binding or activity depending on protein class.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification strategy:\u003c\/strong\u003e Ion-exchange Purified. Purification method and formulation help determine sample homogeneity and background in downstream biochemical assays.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents can support controlled experiments such as reconstitution of molecular interactions, quantitative calibration, and mechanistic perturbation studies with defined inputs. Interpreting outcomes typically benefits from pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex formation.\u003c\/p\u003e","brand":"StressMarq Biosciences Inc.","offers":[{"title":"100 ug","offer_id":53016290787693,"sku":"SPR-444B","price":385.0,"currency_code":"USD","in_stock":true},{"title":"100 ug x 2","offer_id":53016290820461,"sku":"SPR-444C","price":690.0,"currency_code":"USD","in_stock":true},{"title":"100 ug x 5","offer_id":53016290853229,"sku":"SPR-444E","price":1435.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/SPR-444_Tau-Protein-Monomer-Protein-Thioflavin-T-assay-1.png?v=1770644818","url":"https:\/\/www.ebiohippo.com\/products\/tau-dgae-297-391-monomers-bhp11901141","provider":"BioHippo","version":"1.0","type":"link"}