Parkinson's disease (PD) is predominantly a movement disorder resulting from degeneration of dopaminergic neurons in the substantia nigra. The cause of the disease is unknown, but substantial evidence suggests that the aggregation of α-synuclein is a critical step in the etiology of PD. α-Synuclein is an abundant brain protein of 140 residues that is present in high concentration at presynaptic terminals and is found in both soluble and membrane-associated fractions of the brain. Several possible functions have been suggested, among which are vesicle release and trafficking. In vitro incubation in the presence of salt (i.e. 0.1M NaCl) with agitation causes α-synuclein to form fibrils.
The recombinant human α-synuclein (1-140) (GenBank Accession # NP_000336) was expressed and purified from E. coli and conjugated with the fluorescence dye HiLyte™ Fluor 488. Green fluorescence: Excitation/Emission wavelengths= 503 nm/525 nm