Amyloid Beta

StressMarq Biosciences has developed an extensive range of fibrillar, oligomeric and monomeric protein preparations for use in neurodegenerative disease research including alpha synucleinbeta synucleingamma synucleintauamyloid betaSOD1 and TTR. Our goal is to be the world leader in the development and supply of active, pathology-inducing protein aggregates to assist scientists with disease model development and accelerate neurodegenerative disease drug discovery.

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).

Amyloid Beta Pre-formed Fibrils (PFFs), Oligomers, & Monomers 

StressMarq is pleased to offer a variety of amyloid beta protein constructs for neurodegenerative disease research.


Product List | Amyloid Beta

Human Amyloid Beta Pyroglutamate 3-42 Pre-formed Fibrils (PFFs), catalog# SPR-492
Human Amyloid Beta 1-42 Pre-formed Fibrils (PFFs), catalog# SPR-487
Human Amyloid Beta 1-42 Oligomers, catalog# SPR-488
Human Amyloid Beta 1-42 Peptide (HFIP, monomeric), catalog# SPR-485

 

Selected Scientific & Product Information

Structure

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).  Our Amyloid Beta 1-42 (Aβ42) Oligomers and  Amyloid Beta 1-42 (Aβ42) Pre-formed Fibrils (PFFs) are generated from this Amyloid Beta Peptide 1-42 (Aβ42) using a previously published method (1,2).

Upon resuspension in DMSO/dH2O, our Aβ42 presents as a monomeric peptide without fibrils when observed under TEM, AFM and on a Western Blot with an anti-amyloid beta antibody. StressMarq’s Aβ42 PFFs 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 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.


TEM of amyloid beta 1-42 monomers (SPR-485, left), oligomers (SPR-488, middle) and fibrils (SPR-487, right).TEM of Amyloid Beta Peptide Protein (Monomers, Oligomers, and PFFS) (SPR-485, SPR-488, SPR-487)

 

AFM of amyloid beta 1-42 monomers (SPR-485, left), oligomers (SPR-488, middle) and fibrils (SPR-487, right).AFM of Amyloid Beta Peptide Protein (Monomers, Oligomers, and PFFS) (SPR-485, SPR-488, SPR-487)

 

 

 

 

Toxicity

StressMarq’s Amyloid Beta 1-42 oligomers, pre-formed fibrils (PFFs) and monomeric peptide can be used for neurodegenerative disease research.

Amyloid Beta 1-42 Oligomers (catalog# SPR-488) and Amyloid Beta 1-42 PFFs (catalog# SPR-487) show a dose-dependent toxicity to primary rat cortical neurons, whereas our Amyloid Beta 1-42 Peptide (monomeric) (catalog# SPR-485) does not show toxicity.

The charts below show 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.

Amyloid Beta Toxicity Charts

Vehicle controls consisted of buffer without amyloid beta 1-42. Sonication (Bioruptor) was only performed on fibrils and respective vehicle controls. Test conditions were run in the same plate as respective controls. Data expressed as mean +/- s.e.m. (n=6) and statistics determined by 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.

 

 

 

 

 

 

 

 

 

 

 

 


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.2012.1608


Product Citations

StressMarq’s proteins for neurodegenerative disease research have been cited in many peer-reviewed scientific journals. Below is a list of the most recent product citations for our amyloid beta proteins. A complete list of citations for amyloid beta proteins can be seen here.

Most Recent Amyloid Beta Citations

  • High-molecular-weight oligomer tau (HMWoTau) species are dramatically increased in Braak-stage dependent manner in the frontal lobe of human brains, demonstrated by a novel oligomer Tau ELISA with a mouse monoclonal antibody (APNmAb005). Fukumoto, H. et al. FASEB J. 2024.
  • Hybrid amyloid quantum dot nano-bio assemblies to probe neuroinflammatory damage. Chiang, W. et al. ACS Chem Neurosci. 2024.
  • Ultrasensitive detection of aggregated α-synuclein using quiescent seed amplification assay for the diagnosis of Parkinson’s disease. Mao, H. et al. Transl Neurodegener. 2024.

Supplemental Learning Materials

Technical Support Resources

Selected Media from the StressMarq YouTube Channel 

Selected Articles from the StressMarq Blog


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