Tau-441 (2N4R) P301S Mutant Pre-formed Fibrils (CHO-expressed, N-glycosylated)
SKU: BTL-SM-P-00299 |
Brand: Stressmarq
Product Description
| Cat Number | SPR-516XE |
|---|---|
| Category | Recombinant Protein |
| Pack Size | 500 µg (@5mg/ml) |
| Description | Human Recombinant Tau-441 (2N4R) P301S Mutant Pre-formed Fibrils (CHO-expressed, N-glycosylated) |
| Applications | WB | In vivo Assay | In vitro Assay |
| Target | Tau-441 (2N4R) P301S Mutant Pre-formed Fibrils (CHO-expressed, N-glycosylated) |
| Molecular Weight | 48.609 kDa |
| Purity | >95% |
| Research Area | Neuroscience | Neurodegeneration | Alzheimer's Disease | Tangles & Tau |
| Swiss Prot | P10636-8 |
| Scientific Background | Mammalian N-glycosylation is present on CHO-secreted tau 2N4R, which contributes to slower migration on SDS-PAGE than E.coli or Baculovirus/Sf9 expressed tau (1, 2). N-glycosylated tau has been identified in human AD-diseased brains, but not healthy brains, and may precede tau hyperphosphorylation (3, 4). N-glycosylation of Tau has been demonstrated to affect its aggregation propensity (5). The tau P301S mutation is associated with early onset neurodegeneration, and functionally reduces microtubule assembly and stimulates fibril assembly (6, 7). Our CHO-expressed Tau 2N4R P301S will readily form fibrils in the absence of heparin and contains mammalian post-translational modifications that may better mimic tau in human AD-brains. |
| Expression System | Chinese Hamster Ovary (CHO) |
| Protein Length | 441 aa (excluding tag), 466 aa (including tag) |
| Amino Acid Sequence | GGSHHHHHHHHHHGSGGSENLYFQGMAEPRQEFEVMEDHAGTYGLGDRKDQGGYTMHQDQEGDTDAGLKESPLQTPTEDGSEEPGSETSDAKSTPTAEDVTAPLVDEGAPGKQAAAQPHTEIPEGTTAEEAGIGDTPSLEDEAAGHVTQARMVSKSKDGTGSDDKKAKGADGKTKIATPRGAAPPGQKGQANATRIPAKTPPAPKTPPSSGEPPKSGDRSGYSSPGSPGTPGSRSRTPSLPTPPTREPKKVAVVRTPPKSPSSAKSRLQTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVSGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMVDSPQLATLADEVSASLAKQGL |
| Purification | Affinity Purified and Size Exclusion |
| Storage | -80ºC |
| References | 1. Guo et al., 2019. A pathogenic tau fragment compromises microtubules, disrupts insulin signaling and induces the unfolded protein response. Acta Neuropathologica Communications. DOI: 10.1186/s40478-018-0651-9 2. Losev et al., 2020. Differential effects of putative N-glycosylation sites in human Tau on Alzheimer’s disease-related neurodegeneration. Cellular and Molecular Life Sciences. DOI: 10.1007/s00018-020-03643-3 3. Zhang et al., 2020. Integrative glycoproteomics reveals protein N-glycosylation aberrations and glycoproteomic network alterations in Alzheimer’s disease. Sci. Adv. DOI: 10.1126/sciadv.abc5802 4. Liu et al., 2002. Role of glycosylation in hyperphosphorylation of tau in Alzheimer’s disease. FEBS. DOI: 10.1016/S0014-5793(02)02228-7 5. Losev et al., 2019. Novel model of secreted human tau protein reveals the impact of the abnormal N-glycosylation of tau on its aggregation propensity. Sci. Rep. https://doi.org/10.1038/s41598-019-39218-x 6. Bugiani et al., 1999. Frontotemporal Dementia and Corticobasal Degeneration in a Family with a P301S Mutation in Tau. J Neuropathol Exp Neurol. doi: 10.1097/00005072-199906000-00011. 7. Goedert and Crowther, 1999. Effects of frontotemporal dementia FTDP-17 mutations on heparin-induced assembly of tau filaments. FEBS Lett. DOI: 10.1016/s0014-5793(99)00508-7 |
| Product Url | View Document |
| Note | The product is for research use only |
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