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Proteins and Peptides

Amyloid Beta 1-42 Pre-formed Fibrils

Product Size(s)
100 ug
£567.00
SPR-487-100UG
2 x 100 ug
£836.00
SPR-487-2X100UG
5 x 100 ug
£1576.00
SPR-487-5X100UG
Academic Pricing
Please contact us for academic pricing.
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About this Product
SKU:
SPR-487
Additional Names:
Alpha synuclein pre-formed fibrils, Alpha synuclein aggregates, Alpha synuclein protein aggregates, Active Alpha synuclein aggregates, Alpha-synuclein protein, Non-A beta component of AD amyloid protein, Non-A4 component of amyloid precursor protein, NACP protein, SNCA protein, NACP protein, PARK1 protein, SYN protein, Parkison disease familial 1 Protein
Application:
Cell-based/Functional Assay, Western Blot
CE/IVD:
Not for use in humans. Not for use in diagnostics or therapeutics. For research use only.
Extra Details:
Our Amyloid Beta 1-42 (AB Beta42) 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 AB Beta42 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 AB Beta42 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 (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 (2) and SH-SY5Y cells (5). AB Beta was demonstrated to interact with tauopathies to affect neurodegeneration in AD patients (6) and accumulations of AB Beta were shown to be associated with lower survival rates in Parkinson's disease patients with dementia (7).
Molecular Weight:
4.5 kDa
Purity:
>95%
Sequence:
MDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSKTKEGVVH GVATVAEKTK EQVTNVGGAV VTGVTAVAQK TVEGAGSIAA ATGFVKKDQL GKNEEGAPQE GILEDMPVDP DNEAYEMPSE EGYQDYEPEA
Shipping Conditions:
Dry Ice
Storage Conditions:
-70[o]C
Supplier:
StressMarq Biosciences
Type:
Proteins, Peptides, Small Molecules & Other Biomolecules: Synthetic
  • Manufacturer's Data Sheet:
Epitope Tag:
Untagged
TEM of amyloid beta 1-42 fibrils (SPR-487). 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 fibrils (SPR-487). 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.
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 show distinct dimer/trimer bands as well as a signal from ~37-75 kDa (middle). Fibrils observed under TEM/AFM show a signal greater than 100 kDa and a distinct signal 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.