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| Product Name | Amyloid Beta Peptide 1-42 Monomers | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Description |
Human Synthetic Amyloid Beta Peptide 1-42 (HFIP treated) Monomers |
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| Applications | WB, In vivo Assay, In vitro Assay | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Concentration | N/A - dried peptide film | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Conjugates |
No tag
StreptavidinProperties:
Biotin
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| Nature | Synthetic | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Species | Human | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Expression System | Synthetic | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Amino Acid Sequence | DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Purity | >98% | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Other Resources | Protocol for re-suspension of Amyloid Beta Peptide 1-42 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Protein Length | 42 amino acids | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Protein Size | 4.5 kDa | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Field of Use | Not for use in humans. Not for use in diagnostics or therapeutics. For in vitro research use only. | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Properties
| Storage Buffer | Dry powder. See "Other Resources" for re-suspension instructions/protocol. |
| Storage Temperature | -80ºC |
| Shipping Temperature | Blue Ice or 4ºC |
| Purification | N/A |
| Cite This Product | Human Synthetic Amyloid Beta Peptide 1-42 Monomers (StressMarq Biosciences | Victoria, BC CANADA | Catalog# SPR-485) |
| Certificate of Analysis | Certified >98% pure using mass spec and HPLC. |
| Other Relevant Information | For corresponding PFFs, see catalog# SPR-487. For oligomers, see catalog# SPR-488. |
Biological Description
| Alternative Names | Aβ 1-42, Amyloid beta, Beta amyloid peptide, Abeta, Abeta peptide, Amyloid beta precursor peptide, APP, Beta-APP42, Abeta42, A4, ABPP, APPI, Alzheimer disease amyloid A4, Alzheimer disease amyloid, Cerebral vascular amyloid peptide, PreA4, Protease nexin-II, PN-II |
| Research Areas | Alzheimer's Disease, Amyloid, Neurodegeneration, Neuroscience |
| Cellular Localization | Cell membrane, Intracellular Vesicles |
| Gene ID | 351 |
| Swiss Prot | P05067 |
| Scientific Background |
Amyloid beta (Aβ) peptides, derived from the proteolytic cleavage of the amyloid precursor protein (APP), are central to the pathology of Alzheimer’s disease. Among these, the 42-residue variant (Aβ 1-42) is particularly aggregation-prone and neurotoxic. In its monomeric form, Aβ 1-42 plays a critical role in the early stages of disease progression, serving as the molecular seed for oligomer and fibril formation. Aβ 1-42 monomers exhibit distinct biochemical properties, including a higher hydrophobicity and β-sheet propensity compared to shorter isoforms like Aβ 1-40. These features make Aβ 1-42 more likely to misfold and self-assemble into soluble oligomers and insoluble fibrils, which accumulate as amyloid plaques in the brain. Even before aggregation, monomeric Aβ can disrupt synaptic function, induce oxidative stress, and trigger inflammatory responses. In neurodegenerative disease research, Aβ 1-42 monomers are essential for modeling the initiation of amyloidogenesis. Their use in in vitro and in vivo systems enables detailed investigation of misfolding kinetics, membrane interactions, and neurotoxicity. These monomers also serve as a baseline for evaluating therapeutic strategies aimed at stabilizing native Aβ, preventing aggregation, and mitigating early neuronal damage. By capturing the earliest molecular events in Alzheimer’s pathology, Aβ 1-42 monomers provide a foundational platform for advancing biomarker discovery and the development of disease-modifying treatments. StressMarq's amyloid beta peptide 1-42 (Aβ42) is produced synthetically and treated with 1,1,1,3,3,3-Hexafluoro-2-propanol (HFIP) prior to drying which breaks down pre-formed fibrils and monomerizes the peptide, as previously published (1,2). Upon resuspension in Ammonium hydroxide (NH4OH), StressMarq's Aβ42 presents as a monomeric peptide without fibrils when observed under TEM, AFM and on a Western Blot with an anti-amyloid beta antibody. In contrast to AB42 oligomer and fibril constructs, Aβ42 monomers are not toxic to primary rat cortical neurons. |
| 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 Images
TEM of amyloid beta 1-42 monomers (SPR-485, left), oligomers (SPR-488, middle) and fibrils (SPR-487, right). Negative stain transmission electron microscopy images acquired at 80 Kv on carbon coated 400 mesh copper grids using phosphotungstic acid and uranyl acetate stain. Scale bar = 100 nm.
AFM of amyloid beta 1-42 monomers (SPR-485, left), oligomers (SPR-488, middle) and fibrils (SPR-487, right). Atomic force microscopy analysis of 1.0 mg/mL samples diluted to 0.1 mg/mL in dH2O, mounted on freshly cleaved mica, washed, dried and analyzed with tapping mode. Representative images are 2.5 x 2.5 µm x-y with a z-range of 10 nm.
Western blot of amyloid beta 1-42 monomers (SPR-485, left), oligomers (SPR-488, middle) and fibrils (SPR-487, right) using anti-amyloid beta 6E10 antibody. Amyloid beta constructs at 160 pmol were run on 4-12% Bis-Tris SDS-PAGE, transferred to nitrocellulose in the presence of 0.02% v/v Tween-20, and blotted with 1:1000 mouse 6E10 primary antibody (Biolegend). Oligomers observed under TEM/AFM appear as distinct dimer/trimer bands at ~37-75 kDa on Western Blot with 6E10 antibody (middle). Fibrils observed under TEM/AFM appear as a distinct signal at greater than 100 kDa in the stacking gel (right).
Amyloid beta 1-42 oligomers (SPR-488) and fibrils (SPR-487) show a dose-dependent toxicity to primary rat cortical neurons, but not monomers (SPR-485). Survival of rat primary cortical neurons 14 days after treatment with different concentrations of (A) monomers, (B) oligomers or (C) fibrils quantified by MAP2 positive neurons and expressed as a percentage of control. Fibrils and respective vehicle controls were initially sonicated in a Bioruptor. Test conditions were run in the same plate as untreated control and vehicle controls, which consisted of buffer without amyloid beta 1-42 protein. Data expressed as mean +/- s.e.m. (n=6). A global analysis of the data was performed using a one-way ANOVA followed by Dunnett’s test; ** p<0.01 stats vs control; ## p<0.01, #### p<0.0001 stats vs vehicle control. § represents untreated control condition.
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