Product Description
| Cat Number | SPR-487B |
|---|---|
| Category | Recombinant Protein |
| Pack Size | 100 µg |
| Description | Human Synthetic Amyloid Beta 1-42 Pre-formed Fibrils |
| Applications | WB | In vivo Assay | In vitro Assay |
| Target | Amyloid Beta |
| Molecular Weight | 4.5 kDa |
| Cellular Localization | Cell Membrane | Intracellular Vesicles |
| Purity | >95% |
| Research Area | Neuroscience | Neurodegeneration | Alzheimer's Disease | Amyloid |
| Swiss Prot | P05067 |
| Scientific Background | Our Amyloid Beta 1-42 (Aβ42) Pre-formed Fibrils are generated from Amyloid Beta Peptide 1-42 pre-treated with 1,1,1,3,3,3-Hexafluoro-2-propanol (HFIP) using a previously published method (1,2). Our Aβ42 fibrils present as long strands when observed under TEM and AFM, and have a unique high molecular weight signal on a Western Blot with an anti-amyloid beta antibody. Our Aβ42 fibrils were also demonstrated to be toxic to primary rat cortical neurons in a dose-dependent manner after an initial sonication step. In the brain, amyloid beta peptide (Aβ) is generated by protease cleavage of amyloid precursor protein (APP), which aggregates into oligomers, protofibrils, fibrils and ultimately plaques in neurodegenerative diseases. The accumulation of Aβ plaques in the brain is considered a hallmark of Alzheimer’s disease (AD), and most of the drugs tested for AD in the past 20 years have targeted amyloid beta accumulation (3). Soluble Aβ oligomers isolated from the brains of AD patients or those generated in vitro potently impaired synapse structure and function (4). Aβ oligomers generated in vitro were toxic to PC12 cells (2) and SH-SY5Y cells (5). Aβ was demonstrated to interact with tauopathies to affect neurodegeneration in AD patients (6) and accumulations of Aβ were shown to be associated with lower survival rates in Parkinson’s disease patients with dementia (7). |
| Expression System | N/A |
| Gene Id | 351 |
| Protein Length | 42 amino acids |
| Amino Acid Sequence | MDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSKTKEGVVH GVATVAEKTK EQVTNVGGAV VTGVTAVAQK TVEGAGSIAA ATGFVKKDQL GKNEEGAPQE GILEDMPVDP DNEAYEMPSE EGYQDYEPEA |
| Purification | N/A |
| Storage | -80ºC |
| References | 1. Stine et al. 2003. JBC. 278(13):11612-22. doi: 10.1074/jbc.M210207200 2. Chromy et al. 2003. Biochemistry. 42:12749-12760. doi: 10.1021/bi030029q 3. Panza et al. 2019. Nat Rev Neurol. 15:73-88 https://doi.org/10.1038/s41582-018-0116-6 4. Shankar et al. 2008. Nat Med. 14(8):837-842. doi: 10.1038/nm1782 5. Kayed et al. 2003. Science. 300(5618): 486-489. doi: 10.1126/science.1079469 6. Want et al. 2016. JAMA Neurol. 73(9):1070-7. doi: 10.1001/jamaneurol.2016.2078 7. Kotzbauer et al. 2012. Arch Neurol. 69(10): 1326-1331. doi: 10.1001/archneurol.2012.1608 |
| Product Url | View Document |
| Note | The product is for research use only |
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