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Creative Biolabs

Alpha-Synuclein Aggregation Assay Service

Advance your research with our suite of cutting-edge α-synuclein (α-syn) aggregation detection technologies. From basic research to drug discovery, we offer comprehensive solutions to precisely analyze α-synuclein aggregation states, empowering you to explore disease mechanisms, identify early diagnostic markers, and screen potential therapeutics. For further information regarding the products and services provided, project-specific consultation, and pricing, please submit an inquiry here.

Introduction

Abnormal aggregation of α-synuclein. (Calabresi, et al., 2023) Fig.1 α-Syn aggregates in SH-SY5Y cells.

Abnormal aggregation of α-synuclein is a key pathological feature of neurodegenerative diseases such as Parkinson's disease (PD), dementia with Lewy bodies (DLB), and multiple system atrophy (MSA). α-Synuclein is a 140-amino acid protein that is mainly expressed in the presynaptic terminals and synaptic vesicles of neurons and is involved in neurotransmitter release and synaptic signaling. It is highly soluble and hydrophilic and can interact with phospholipids and proteins. In addition, α-Syn exists as a monomer under normal physiological conditions but forms oligomers, fibrillar fibrils, and amyloid fibrils under pathological conditions. The dynamic formation process of its aggregates (e.g., monomer → oligomer → fibril → Lewy body) is closely linked to neuronal toxicity.

α-Syn Aggregation Assays

  • Cell Models

Streamline your drug development pipeline with our rapid and reliable α-synuclein aggregation assay. In our α-synuclein aggregation assay, we used SH-SY5Y cells stably overexpressing α-synuclein. Intracellular α-syn aggregation can be induced by treating cells with preformed recombinant α-syn fibrils (PFFs). The model quantifies the aggregation effect by the following four indicators:

  • Number of aggregates per cell
  • Size of aggregates
  • Fluorescence intensity of aggregates
  • Percentage of cells containing aggregates

These indicators can be used for high-throughput screening of compounds that inhibit α-syn propagation, and the experimental cycle is short (24 hours), which is suitable for drug development.

Fig.1 α-Syn aggregates in SH-SY5Y cells. Fig.1 α-Syn aggregation in SH-SY5Y cells.2, 3

  • Mechanism of Induced Aggregation

Investigate the intricate mechanisms of α-synuclein propagation with our specialized research tools. We offer a comprehensive suite of products designed to facilitate your studies of prion-like seeding, a critical process in the development of PD and other synucleinopathies.

Fig.2 Prion-like seeding. (Creative Biolabs Original)

  • Real-Time Monitoring: Track α-synuclein fibril formation in real time with our high-quality Thioflavin T (ThT) reagent.
  • Comprehensive Detection: Utilize our optimized Western blot and amyloid fluorescent staining protocols for accurate detection and analysis of intracellular α-synuclein aggregates.
  • Validated Models: Our tools are compatible with various cell models, allowing you to study prion-like seeding in a physiologically relevant context.

Our α-syn aggregation assay is suitable for a variety of sample types, including cell culture, brain extracts, and biological fluids (such as serum, cerebrospinal fluid, etc.), which can meet different research needs. We also provide customized detection solutions that support a variety of sample types and experimental conditions. Please contact us to accelerate your research.

References

  1. Calabresi, Paolo, et al. "Alpha-synuclein in Parkinson's disease and other synucleinopathies: from overt neurodegeneration back to early synaptic dysfunction."Cell death & disease 14.3 (2023): 176.
  2. Sang, Jason C., et al. "Super-resolution imaging reveals α-synuclein seeded aggregation in SH-SY5Y cells." Communications biology 4.1 (2021): 613.
  3. Distributed under Open Access license CC BY 4.0, without modification.
For Research Use Only. Not For Clinical Use.
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