Product Description
| Cat Number | SPR-488C |
|---|---|
| Category | Recombinant Protein |
| Pack Size | 100 µg x2 |
| Description | Human Synthetic Amyloid Beta 1-42 Oligomers |
| Applications | WB | In vivo Assay | In vitro Assay |
| Target | Amyloid Beta Oligomers |
| 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) Oligomers are generated from Amyloid Beta Peptide 1-42 pre-treated with 1,1,1,3,3,3-Hexafluoro-2-propanol (HFIP) as previously published (1,2). Our Aβ42 oligomers present as globular oligomers when observed under TEM and AFM, and have a unique dimer/trimer and oligomer signal on a Western Blot with an anti-amyloid beta antibody. Our Aβ42 oligomers were also demonstrated to be toxic to primary rat cortical neurons in a dose-dependent manner. 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 (5) and SH-SY5Y cells (6). Aβ was demonstrated to interact with tauopathies to affect neurodegeneration in AD patients (7) and accumulations of Aβ were shown to be associated with lower survival rates in Parkinson’s disease patients with dementia (8). |
| Expression System | N/A |
| Gene Id | 351 |
| Protein Length | 42 amino acids |
| Amino Acid Sequence | DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA |
| Purification | N/A |
| Storage | -80ºC |
| References | 1. Stine et al. 2003. JBC. 278(13):11612-22. doi: 10.1074/jbc.M210207200 2. Ahmed et al. 2010. Nature Structural & Molecular Biology. 17(5):561-7. doi: 10.1038/nsmb.1799 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. Chromy et al. 2003. Biochemistry. 42:12749-12760. doi: 10.1021/bi030029q 6. Kayed et al. 2003. Science. 300(5618): 486-489. doi: 10.1126/science.1079469 7. Want et al. 2016. JAMA Neurol. 73(9):1070-7. doi: 10.1001/jamaneurol.2016.2078 8. Kotzbauer et al. 2012. Arch Neurol. 69(10): 1326-1331. doi: 10.1001/archneurol.2012.1610 |
| Product Url | View Document |
| Note | The product is for research use only |
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