Tau-441 (2N4R) and Alpha Synuclein Co-Polymer Fibrils
SKU: BTL-SM-P-00229 |
Brand: Stressmarq
Product Description
| Cat Number | SPR-495E |
|---|---|
| Category | Recombinant Protein |
| Pack Size | 100 µg x5 |
| Description | Human Recombinant Tau-441 (2N4R) and Human Recombinant Alpha Synuclein Co-Polymer Fibrils |
| Applications | WB | SDS PAGE | In vitro assay |
| Target | Tau and Alpha Synuclein Co-Polymer |
| Molecular Weight | 2N4R: 45.84 kDa, ASYN: 14.46 kDa |
| Purity | >95% |
| Research Area | Neuroscience | Neurodegeneration | Alzheimer's Disease | Tangles & Tau | Neuroscience | Neurodegeneration | Parkinson's Disease | Synuclein | Neuroscience | Neurodegeneration | Multiple System Atrophy |
| Swiss Prot | P10636-8 and P37840-1 |
| Scientific Background | Brain-specific tau isoforms vary in the number of N-terminal inserts and C- terminal repeat domains due to alternative splicing of exons; the 2N4R isoform of tau is expressed in adult brain yet is absent from the fetal brain (1). Tau and alpha-synuclein polymerize into amyloid fibrils to form filamentous inclusions in neurodegenerative diseases such as Alzheimer’s and Parkinson’s disease. Tau has been shown to interact with alpha-synuclein in vitro (2), with synergistic cross-seeding between tau and alpha-synuclein resulting in polymerization of each other into fibrillary amyloid lesions in neuronal cultures and in vivo (3,4). Recombinant tau and alpha-synuclein co-polymer fibrils have demonstrated a more widespread transmission of induced pathology in a rodent model of tauopathies compared to pure Tau or alpha-synuclein fibrils alone (5). These co-polymer fibrils have also shown enhanced alpha-synuclein aggregation in vitro, and more severe alpha-synuclein pathology and Parkinson’s disease-like symptoms in mice (6). |
| Expression System | E. coli |
| Protein Length | Full Length (Tau 2N4R: 1-441 aa, ASYN: 1-140 ) |
| Amino Acid Sequence | Tau: MAEPRQEFEVMEDHAGTYGLGDRKDQGGYTMHQDQEGDTDAGLKESPLQTPTEDGSEEPGSETSDAKSTPTAEDVTAPLVDEGAPGKQAAAQPHTEIPEGTTAEEAGIGDTPSLEDEAAGHVTQARMVSKSKDGTGSDDKKAKGADGKTKIATPRGAAPPGQKGQANATRIPAKTPPAPKTPPSSGEPPKSGDRSGYSSPGSPGTPGSRSRTPSLPTPPTREPKKVAVVRTPPKSPSSAKSRLQTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMVDSPQLATLADEVSASLAKQGL Asyn: MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA |
| Purification | Ion-exchange Purified |
| Storage | -80ºC |
| References | 1. 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. 2. Jensen et al. α-synuclein Binds to Tau and Stimulates the Protein Kinase A-catalyzed Tau Phosphorylation of Serine Residues 262 and 356. 1999. JBC. 274(36): 25481-25489. DOI:https://doi.org/10.1074/jbc.274.36.25481 3. Giasson et al. Initiation and Synergistic Fibrillization of Tau and Alpha-Synuclein. Science. 2003; 300: 636-40. DOI: 10.1126/science.1082324 4. Guo et al. Distinct α-synuclein Strains Differentially Promote Tau Inclusions in Neurons. 2013. Cell. 154(1) doi:10.1016/j.cell.2013.05.057. 5. Williams et al. Differential Cross-seeding Properties of Tau and α-synuclein in Mouse Models of Tauopathy and Synucleinopathy. Brain Communications. 2020; 2(2):fcaa090. doi:10.1093/braincomms/fcaa090 6. Pan et al. Tau Accelerates α-synuclein Aggregation and Spreading in Parkinson’s Disease. 2022. Brain. Doi: 10.1093/brain/awac171 |
| Product Url | View Document |
| Note | The product is for research use only |
Share Item: