Scientific Background: A 15 amino acid tag on the C-terminal tail of Alpha Synuclein facilitates site-specific covalent biotinylation (1). Biotinylation of purified alpha synuclein allows for many biological applications, such as monitoring and detection using streptavidin-based conjugates (1, 2, 3). Our biotinylated monomers are also used to generate pre-formed fibrils in-vitro.
References: 1.Fairhead & Howarth. 2015. Site-specific biotinylation of purified proteins using BirA. Methods in Molecular Biology. DOI: 1007/978-1-4939-2272-7_122.Hallacli et al. 2022. The Parkinson’s disease protein alpha synuclein is a modulator of Processing-bodies and mRNA stability. Cell. DOI: 10.1016/j.cell.2022.05.0083.Li et al. 2019. Naturally occurring antibodies isolated from PD patients inhibit synuclein seeding in vitro and recognize Lewy pathology. Acta neuropathologica. DOI: 10.1007/s00401-019-01974-5.
Field of Use: Not for use in humans. Not for use in diagnostics or therapeutics. For research use only.