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α-Synuclein (human), (recombinant)

ALX-201-265-C100 100 µg 349.00 USD
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Replaces Prod. #: BML-SE256

Product Details

MW:~14.5kDa (MW in SDS-PAGE will be shifted up).
Source:Produced in E. coli.
UniProt ID:P37840
Formulation:Liquid. In 20mM TRIS-HCl, pH 7.5, containing 0.1M sodium chloride and 1mM magnesium dichloride.
Purity:≥95% (SDS-PAGE)
Endotoxin Content:<1.0EU/µg of protein (LAL method).
Shipping:Blue Ice
Long Term Storage:-20°C
Handling:Avoid freeze/thaw cycles.
Scientific Background:α-synuclein is a major component of Parkinson’s disease aggregates and is implicated in the pathogenesis of Parkinson’s disease and related neurodegenerative disorders. α-synuclein accumulates in the brains of sporadic Parkinson’s disease patients as a major component of Lewy bodies, which are intraneuronal cytoplasmic inclusions characteristic of Parkinson’s disease. α-synuclein appears to associate with other proteins that aggregate and is found in β-amyloid plaques and neuritic tangles in Alzheimer’s disease.
Regulatory Status:RUO - Research Use Only
&alpha;-Synuclein (human), (recombinant) SDS-PAGE
Figure: 14% SDS-PAGE of α-Synuclein (human) (rec.) (Prod. No. ALX-201-265)."
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&alpha;-Synuclein (human), (recombinant) SDS-PAGE

Product Literature References

Engineered graphene quantum dot nanocomposite triggers α-synuclein defibrillation: Therapeutics against Parkinson's disease: P. Kaliyaperumal, et al.; Nanomedicine 47, 102608 (2023), Abstract;
Dopaminergic Toxin 1-Methyl-4-Phenylpyridinium, Proteins α-Synuclein and Glia Maturation Factor Activate Mast Cells and Release Inflammatory Mediators: D. Kempuraj, et al.; PLoS One 10, e0135776 (2015), Application(s): Stimulating mouse and human mast cells to release IL-1β, Abstract; Full Text

General Literature References

Neurobiology of alpha-synuclein : K. Vekrellis, et al.; Mol. Neurobiol. 30, 1 (2004), (Review), Abstract;
beta-amyloid peptides enhance alpha-synuclein accumulation and neuronal deficits in a transgenic mouse model linking Alzheimer's disease and Parkinson's disease: E. Mashliah et al.; PNAS 98, 12245 (2001), Abstract;
Fibrils formed in vitro from alpha-synuclein and two mutant forms linked to Parkinson's disease are typical amyloid: K.A. Conway et al.; Biochemistry 39, 2552 (2000), Abstract;
.: R. Jakes et al.; FEBS Lett. 345, 27 (1994), Abstract;
Molecular cloning of cDNA encoding an unrecognized component of amyloid in Alzheimer disease: K. Ueda et al.; PNAS 90, 11282 (1993), Abstract;

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