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Proteins and Peptides

Amyloid Beta 1-42 Oligomers

Product Sizes
100 ug
SPR-488-100UG
2 x 100 ug
SPR-488-2X100UG
5 x 100 ug
SPR-488-5X100UG
About this Product
SKU:
SPR-488
Additional Names:
Abeta Oligomers, Abeta peptide, Amyloid beta peptide oligomers, Beta amyloid peptide oligomers, amyloid beta precursor protein peptide oligomers, APP
Application:
Cell-based/Functional Assay, Western Blot
CE/IVD:
RUO
Concentration:
1 mg/ml
Extra Details:
Our Amyloid Beta 1-42 (AB Beta42) 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 AB Beta42 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 AB Beta42 oligomers were also demonstrated to be toxic to primary rat cortical neurons in a dose-dependent manner. In the brain, amyloid beta peptide (AB Beta) 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 AB Beta 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 AB Beta oligomers isolated from the brains of AD patients or those generated in vitro potently impaired synapse structure and function (4). AB Beta oligomers generated in vitro were toxic to PC12 cells (5) and SH-SY5Y cells (6). AB Beta was demonstrated to interact with tauopathies to affect neurodegeneration in AD patients (7) and accumulations of AB Beta were shown to be associated with lower survival rates in Parkinson's disease patients with dementia (8).
Immunogen:
Amyloid Beta Oligomers
Molecular Weight:
4.5 kDa
Purity:
>95%
Sequence:
DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA
Shipping Conditions:
Dry Ice
Storage Conditions:
-70[o]C
Supplier:
StressMarq Biosciences
Type:
Proteins, Peptides, Small Molecules & Other Biomolecules: Synthetic
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.
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.
Human iPSC-derived microglia uptake of StressMarq Amyloid Beta 1-42 Oligomers (SPR-488) conjugated to Phrodo dye. Live cell imaging performed by reMYND (Leuven, Belgium) using Ex560 Em585.
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 um x-y with a z-range of 10 nm.