Active alpha-synuclein proteins

Easily induce Lewy body pathology in neurons with active alpha-synuclein protein aggregates and monomers. Suitable for in vitro and in vivo experiments.

Lewy bodies are intraneuronal aggregates of alpha-synuclein protein characteristic of Parkinson’s disease, Lewy body dementia and other disorders. They are found in the regions of the brain responsible for motor control and result in a progressive decline in mental ability.

Figure 1. Alpha-synuclein fibril aggregate formation from the monomeric form.

The advantages of alpha-synuclein proteins

• Induce Lewy body pathology in your experiment ¹
• Detect active endogenous alpha-synuclein levels after addition of monomer or aggregate proteins using thioflavin T or an equivalent beta-sheet binding dye
• Compare your results with alpha-synuclein monomers or aggregate controls
• Explore in vivo and in vitro applications (eg screen drug targets)

Assay alpha-synuclein proteins using thioflavin T (ThT)

Active alpha-synuclein aggregate seeds the formation of new alpha-synuclein aggregates from a pool of active alpha-synuclein monomers. ThT is a fluorescent dye that binds to beta sheet-rich structures, such as those in alpha-synuclein aggregates. Upon binding, the emission spectrum of the dye experiences a red-shift, and increased fluorescence intensity.

Click here for protocol

Products

Further reading

1.        Luk, K. C. & Lee, V. M.-Y. Modeling Lewy pathology propagation in Parkinson’s disease. Parkinsonism Relat. Disord. 20, S85–S87 (2014). Read more

2.        Vieira, B. D. M., Radford, R. A., Chung, R. S., Guillemin, G. J. & Pountney, D. L. Neuroinflammation in Multiple System Atrophy: Response to and Cause of α-Synuclein Aggregation. Front. Cell. Neurosci. 9, 437 (2015). Read more

3.        Roberts, H. & Brown, D. Seeking a Mechanism for the Toxicity of Oligomeric α-Synuclein. Biomolecules 5, 282–305 (2015). Read more

4.        Fernagut, P.-O. & Chesselet, M.-F. Alpha-synuclein and transgenic mouse models. Neurobiol. Dis. 17, 123–130 (2004). Read more

5.        Ariesandi, W., Chang, C.-F., Chen, T.-E. & Chen, Y.-R. Temperature-Dependent Structural Changes of Parkinson’s Alpha-Synuclein Reveal the Role of Pre-Existing Oligomers in Alpha-Synuclein Fibrillization. PLoS One 8, e53487 (2013). Read more