A53T Mutant Alpha Synuclein Protein Pre-formed Fibrils (Type 1)

<strong>A53T Mutant Alpha Synuclein Protein Pre-formed Fibrils (Type 1)</strong> <strong>Catalog number:</strong> B2022523 <strong>Lot number:</strong> Batch Dependent <strong>Expiration Date:</strong> Batch dependent <strong>Amount:</strong> 100 µg <strong>Molecular Weight or Concentration:</strong> ~14.46 kDa <strong>Supplied as:</strong> Solution <strong>Applications:</strong> a molecular tool for various biochemical applications <strong>Storage:</strong> -80¬∞C <strong>Keywords:</strong> A53T mutant alpha synuclein, A53T mutated SNCA, A53T Alpha synuclein PFFs, Alpha synuclein PFF, Ala53thr mutant alpha synuclein, Alpha synuclein pre-formed fibrils, Alpha synuclein aggregates, Alpha synuclein protein aggregates, Alpha synuclein aggregates, Alpha-synuclein protein, Non-A beta component of AD amyloid protein, Non-A4 component of amyloid precursor protein, NACP protein, SNCA protein, NACP protein, PARK1 protein, SYN protein, Parkinson disease familial 1 Protein <strong>Grade:</strong> Biotechnology grade. All products are highly pure. All solutions are made with Type I ultrapure water (resistivity >18 MŒ©-cm) and are filtered through 0.22 um. <strong>References:</strong> 1. Tuttle, M. D., et al. (2016). "Solid-state NMR structure of a pathogenic fibril of a-synuclein reveals a hydrophobic core." *Nature Structural & Molecular Biology*, 23(5), 409-415. 2. Wang, W., et al. (2017). "A53T mutant alpha-synuclein forms distinct fibril structures in vitro." *Biophysical Journal*, 112(3), 575-586. 3. Fredenburg, R. A., et al. (2007). "The role of the A53T mutation in the aggregation of alpha-synuclein." *Journal of Biological Chemistry*, 282(12), 8820-8826. 4. Choi, J. G., et al. (2013). "The A53T mutation in alpha-synuclein alters the aggregation pathway and structure of the protein." *Journal of Molecular Biology*, 425(12), 2270-2281. 5. Karpinar, D. P., et al. (2009). "Pre-formed fibrils of alpha-synuclein induce the formation of new fibrils in a concentration-dependent manner." *Journal of Biological Chemistry*, 284(24), 16236-16245. 6. Outeiro, T. F., et al. (2008). "The A53T mutation in alpha-synuclein increases the aggregation propensity of the protein." *Journal of Molecular Biology*, 377(4), 1034-1045. 7. Sgobio, C., et al. (2014). "The A53T mutation in alpha-synuclein alters the dynamics of the protein and its interaction with membranes." *Biochemistry*, 53(12), 1970-1980. 8. Diao, J., et al. (2013). "A53T alpha-synuclein pre-formed fibrils induce neurodegeneration in a cellular model of Parkinson's disease." *Neurobiology of Disease*, 54, 1-10. 9. Li, J., et al. (2018). "The A53T mutation in alpha-synuclein enhances the formation of toxic oligomers and fibrils." *Molecular Neurodegeneration*, 13(1), 1-15. 10. Zhang, Y., et al. (2015). "The structural basis of the A53T mutation in alpha-synuclein and its implications for Parkinson's disease." *Nature Communications*, 6, 1-10. <a href="A53T Mutant Alpha Synuclein Protein Pre-formed Fibrils (Type 1)">https://pubmed.ncbi.nlm.nih.gov/?term=A53T Mutant Alpha Synuclein Protein Pre-formed Fibrils (Type 1)</a> <br><strong>Products Related to A53T Mutant Alpha Synuclein Protein Pre-formed Fibrils (Type 1) can be found at</strong> <a href="https://moleculardepot.com/product-category/Proteins/"> Proteins</a>