| Storage Buffer | PBS pH 7.4 |
| Storage Temperature | -80ºC |
| Shipping Temperature | Dry Ice. Shipping note: Product will be shipped separately from other products purchased in the same order. |
| Purification | Ion-exchange Purified |
| Cite This Product | Human Recombinant Transthyretin (TTR) Y78F Variant Filaments (StressMarq Biosciences | Victoria, BC CANADA | Catalog# SPR-465) |
| Certificate of Analysis | Certified >95% pure using SDS-PAGE analysis. Low endotoxin <5 EU/mL @ 2mg/mL. |
| Other Relevant Information | For best results, sonicate immediately prior to use. Refer to the Neurodegenerative Protein Handling Instructions on our website, or the product datasheet for further information. Monomer source is catalog# SPR-452. |
| Alternative Names | Transthyretin Y78F, TTR Y78F, ATTR, Amyloid polyneuropathy, Amyloidosis I, Carpal tunnel syndrome 1, CTS, CTS1, HEL111, HsT2651, PALB, Prealbumin, Prealbumin amyloidosis type I, Prealbumin Thyroxine-binding, TBPA, Thyroxine binding prealbumin, TTHY_HUMAN, TTR |
| Research Areas | ALS Disease, Alzheimer's Disease, Blood, Cardiovascular System, Cell Signaling, Lipid and lipoprotein Metabolism, Metabolism, Neurodegeneration, Neuroscience, Parkinson's Disease, Tangles & Tau |
| Cellular Localization | Cytoplasm, Extracellular exosome, Extracellular Region, Lysosome |
| Accession Number | NP_000362.1 |
| Gene ID | 7276 |
| Swiss Prot | P02766 |
| Scientific Background |
Transthyretin (TTR), encoded by the TTR gene (UniProt ID: P02766), is a tetrameric transport protein primarily responsible for carrying thyroxine and retinol-binding protein in plasma and cerebrospinal fluid. Under pathological conditions, TTR can misfold and aggregate into amyloid fibrils, contributing to systemic and neurological disorders. The Y78F mutation involves a substitution of tyrosine with phenylalanine at position 78, a site critical for TTR’s structural stability and interaction with ligands. This variant alters the protein’s folding dynamics, increasing its propensity to dissociate into monomers and form amyloid filaments. These filaments exhibit enhanced stability and aggregation potential, making them a valuable model for studying the molecular mechanisms underlying transthyretin amyloidosis and its neurological manifestations. TTR Y78F filaments are used in experimental systems to investigate protein misfolding, cellular toxicity, and tissue-specific deposition. Their structural fidelity to patient-derived amyloid aggregates enables high-resolution studies of neurodegenerative processes, including oxidative stress, inflammation, and neuronal dysfunction. These filaments also support therapeutic development by providing a consistent platform for screening stabilizers, aggregation inhibitors, and clearance-enhancing agents. As a result, TTR Y78F variant filaments are instrumental in advancing translational research focused on amyloid-related neurodegenerative diseases. |
| References |
1. Zeldenrust S.R., Benson M.D. (2010). Wiley. pp. 795–815. 2. Westermark P., Sletten K., Johansson B., Cornwell G.G. (1990). Proc. Natl. Acad. Sci. U.S.A. 87(7): 2843–5. 3. Andrade C. (1952). Brain. 75(3): 408–27. 4. Coelho T. (1996). Curr. Opin. Neurol. 9(5): 355–9. 5. Jacobson D.R, et. al. (1997). N. Engl. J. Med. 336(7): 466–73. 6. Li X. (2011). Mol Neurodegener. 6(1):79. 7. Terazaki H.,m et al. (2006) Lab Invest. 86(1): 23-31. |
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