Alpha Synuclein
StressMarq Biosciences is a leading provider of high-quality fibrillar, oligomeric, and monomeric protein preparations—including alpha synuclein, tau, amyloid beta, TDP-43, SOD1, TTR and more—designed to support cutting-edge neurodegenerative disease research. With a focus on pathology-inducing protein aggregates, our products support the development of robust disease models and accelerate drug discovery for conditions such as Alzheimer’s, Parkinson’s, and ALS. StressMarq is committed to scientific excellence— empowering researchers worldwide with tools that accelerate discovery and translational research.
Alpha Synuclein Pre-formed Fibrils (PFFs), Oligomers, & Monomers
Alpha synuclein is a highly soluble, intrinsically disordered protein abundantly expressed in the brain, particularly at presynaptic terminals. It plays a key role in synaptic vesicle trafficking and neurotransmitter release, including dopamine—critical for motor function. Misfolded alpha synuclein can aggregate into oligomers and fibrils, which are neurotoxic and capable of spreading pathology in a prion-like manner. These aggregates are central to a group of neurodegenerative disorders known as synucleinopathies, including Parkinson’s disease (PD), dementia with Lewy bodies (DLB), diffuse Lewy body disease (DLBD), and multiple system atrophy (MSA).
StressMarq Biosciences provides a diverse range of monomeric, oligomeric, and fibrillar alpha synuclein constructs—each rigorously characterized for activity, stability, and disease relevance. Our products support the development of robust in vitro and in vivo disease models that replicate key pathological features such as Lewy body formation and pSer129 phosphorylation. Explore our catalog to find the right tools for your research, and watch our video to see how StressMarq’s alpha synuclein reagents can accelerate disease modeling and drug discovery.
Alpha Synuclein Pre-formed Fibrils (PFFs)
StressMarq’s alpha synuclein pre-formed fibrils (PFFs) seed the formation of new fibrils from active alpha synuclein monomers, and can be used to induce endogenous alpha synuclein phosphorylation and subsequent Lewy body inclusion formation in neuronal cell culture or for in vitro oligomerization studies.
Product List | PFFs
Alpha Synuclein & Tau Co-Polymer Fibrils (Mixed Fibrils/PFFs)
StressMarq’s co-polymer fibrils are developed by co-incubating monomers together to form fibrils that contain both tau and alpha synuclein proteins within a single fibril. These co-polymer fibrils have been demonstrated to seed fibril formation of both alpha synuclein monomers and of a mixture of alpha synuclein and tau monomers.
Product List | Co-Polymer Fibrils
Human Tau-352 (fetal 0N3R) & Human Alpha Synuclein Co-Polymer Fibrils, catalog# SPR-494 |
Human Tau-441 (2N4R) & Human Alpha Synuclein Co-Polymer Fibrils, catalog# SPR-495 |
Alpha Synuclein Oligomers
Alpha synuclein oligomers are increasingly thought to be the toxic species in synucleinopathies. StressMarq’s kinetically stable alpha synuclein oligomers are toxic to dopaminergic neurons and induce phosphorylation of alpha synuclein Ser129 (a pathology associated with Parkinson’s disease), and are generated without the addition of any inducers or inhibitors. StressMarq also offers dopamine-stabilized alpha synuclein oligomers and EGCG-stabilized alpha synuclein oligomers. Dopamine and EGCG can be used to stabilize alpha synuclein in its oligomeric forms, preventing further aggregation into fibrils.
Product List | Oligomers
Human Alpha Synuclein Oligomers (Kinetically Stable), catalog# SPR-484 |
Human Alpha Synuclein Oligomers (Dopamine HCl stabilized), catalog# SPR-466 |
Human Alpha Synuclein Oligomers (EGCG stabilized), catalog# SPR-469 |
Alpha Synuclein Monomers
StressMarq’s alpha synuclein monomers are capable of aggregation. They do not show neurodegenerative activity.
Product List | Monomers
Human Alpha Synuclein Monomers (Type 1), catalog# SPR-321 |
Human Alpha Synuclein Monomers (Type 2), catalog# SPR-316 |
Mouse Alpha Synuclein Monomers (Type 1), catalog# SPR-323 |
Human Alpha Synuclein A53T Mutant Monomers (Type 1), catalog# SPR-325 |
Human Alpha Synuclein A90C Mutant Monomers catalog# SPR-478 |
Human Alpha Synuclein E114C Mutant Monomers (ATTO 488 conjugated), catalog# SPR-517-A488 |
Human Alpha Synuclein S87N Mutant Monomers, catalog# SPR-499 |
Human Alpha Synuclein S129A Mutant Monomers, catalog# SPR-505 |
Human Alpha Synuclein TNG (A53T, S87N, N103G) Mutant Monomers, catalog# SPR-503 |
Human Alpha Synuclein N-Terminal Acetylated Monomers (Type 1), catalog# SPR-331 |
Human Alpha Synuclein Monomers: Biotinylated (C-Terminus), catalog# SPR-507 |
Human Alpha Synuclein pSer129 Monomers , catalog# SPR-520 New! |
Rat Alpha Synuclein Monomers, catalog# SPR-481 |
Selected Scientific & Product Information
3D Whole-Brain Imaging of Alpha Synuclein Aggregation Following Pre-formed Fibril (PFF) Injection
In collaboration with Gubra, StressMarq’s Alpha Synuclein PFFs (catalog#SPR-324) were injected into a mouse brain to generate a 3D whole-brain light sheet fluorescence imaging model, depicting alpha synuclein pSer129+ aggregation (shown in magenta) 4 weeks post -injection.
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Cell-to-Cell Transmission of Alpha Synuclein Pre-formed Fibrils (PFFs)
StressMarq’s Alpha Synuclein PFFs catalog#SPR-322 (below in red), were shown to be taken up by SH-SY5Y cells and transmitted to neuronal iPSCs within 14 days.
Secondary Structure of Alpha Synuclein Monomers, Oligomers and Pre-formed Fibrils (PFFs)
Oligomers & Fibrils. UV-CD data suggests that StressMarq’s alpha synuclein oligomers have distinct secondary structure differences compared to our monomers and fibrils. More specifically, our Kinetically Stable Alpha Synuclein Oligomers (cat#SPR-484) show a significantly higher alpha helix content and lower beta sheet/turn content than our Alpha Synuclein Pre-formed Fibrils (Type 1) (cat#SPR-322). Alpha Synuclein Monomers (cat#SPR-316) show a strong negative signal at 200 nm, indicative of a disordered protein state (low secondary structure content).
Type 1 & Type 2 Pre-formed Fibrils. UV-CD data suggests StressMarq’s Alpha Synuclein Pre-formed Fibrils (PFFs), Type 1 (cat#SPR-322) and Type 2 (cat#SPR-317) both have a high beta sheet/turn content, yet do have small secondary structure differences. Alpha Synuclein Monomers (cat#SPR-316) show a strong negative signal at 200 nm indicative of a disordered protein state (low secondary structure content). For this experiment, pre-formed fibrils (PFFs) were subjected to 10 cycles of sonication prior to UV-CD to ensure solubility prior to measurement.

Alpha Synuclein Pre-formed Fibrils (PFFs), Type 1 (cat#SPR-322) and Type 2 (cat#SPR-317) have small secondary structure differences.
Kinetically Stable Alpha Synuclein Oligomers Induce Toxicity & Pathology
Kinetically Stable Alpha Synuclein Oligomers (catalog#SPR-484) are toxic to dopaminergic neurons and induce phosphorylation of alpha synuclein Ser129, a pathology associated with Parkinson’s disease. They are stable after a freeze-thaw cycle and when incubated at 37 degrees celsius for 2 weeks.

Parkinson’s-associated pSer129 pathology induced in rat primary dopaminergic cells by kinetically stable alpha synuclein oligomers (cat#SPR-484).

Kinetically stable alpha synuclein oligomers (cat#SPR-484) show toxicity to rat primary dopaminergic neurons.

Kinetically stable alpha synuclein oligomers (cat#SPR-484) are stable after a freeze-thaw cycle and when incubated at 37 oC for 2 weeks.
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 alpha synuclein proteins. A complete list of citations for alpha synuclein proteins can be seen here.
Most Recent Alpha Synuclein Citations
- Strain-distinct α-synuclein and tau cross-seeding uncovered by correlative approach with optical photothermal infrared sub-micron imaging. Zhan, X. et al. J Am Chem Soc. Aug 2025.
- Catalog# SPR-321: Human Recombinant Alpha Synuclein Monomers (Type 1)
- Catalog# SPR-322: Human Recombinant Alpha Synuclein Pre-formed Fibrils (Type 1)
- Catalog# SPR-494: Human Recombinant Tau-352 (fetal 0N3R) & Human Recombinant Alpha Synuclein Co-Polymer Fibrils
- Catalog# SPR-495: Human Recombinant Tau-441 (2N4R) & Human Recombinant Alpha Synuclein Co-Polymer Fibrils
- Activated TBK1 promotes ACSL1-mediated microglia lipid droplet accumulation and neuroinflammation in Parkinson’s disease. Han, C. et al. J Neuroinflammation. July 2025.
- Catalog# SPR-324: Mouse Recombinant Alpha Synuclein Pre-formed Fibrils (Type 1)
- Development of convolutional neural networks for automated brain-wide histopathological analysis in mouse models of synucleinopathies. Barber-Janer, A. et al. bioRxiv [Preprint]. July 2025.
- Catalog# SPR-324: Mouse Recombinant Alpha Synuclein Pre-formed Fibrils (Type 1)
Supplemental Learning Materials
Technical Support Resources
- Handling Instructions | Synucleins
- Protocols | Alpha Synuclein
- Sonication Protocol | PFFs
- Frequently Asked Questions | Neuro Proteins
Selected Media from the StressMarq YouTube Channel
- Video | Alpha Synuclein Pre-formed Fibrils (PFFs) and Oligomers for Modelling Parkinson’s Disease
- Webinar | Protein Constructs for Neurodegenerative Disease Research | Presented by Dr. Jacob McPhail, Lead R&D Scientist, StressMarq
- Open Theatre | Alpha Synuclein Sonication | Presented Dr. Ariel Louwrier, CEO & President, StressMarq
Selected Articles from the StressMarq Blog
- Alpha Synuclein Fibrillar Constructs | Learn about Type 1 & 2 PFFs, key mutations in PD pathology, and monomeric, fibrillar & oligomeric alpha synuclein.
- Alpha Synuclein Inhibition Using Biomimetic Peptides | Dual-function biomimetic peptides inhibited fibrillization of alpha synuclein in a model of PD pathology.
- A Novel Modifier of Alpha Synuclein-Induced Toxicity | A screen of Drosophila identified GPAT as a potent modifier of alpha synuclein cytotoxicity.
- Treating Alpha Synuclein Pathology with NOX Inhibitors | Compound-11 is an NADPH oxidase (NOX) inhibitor that reduces alpha synuclein aggregation in PD models.
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