Alpha Synuclein Pre-formed Fibrils: Biotinylated (C-terminus)

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.

Alpha synuclein, Alpha-synuclein pre-formed fibril, Alpha synuclein protein PFF, Alpha synuclein PFF, Alpha-synuclein protein, Non-A beta component of AD amyloid protein, Non-A4 component of amyloid precursor protein, NACP protein, SNCA protein, NACP protein, PARK1 protein, SYN protein, Parkinson disease familial 1 Protein

MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVH GVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQL GKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEAGLNDIFEAQK IEWHE

For best results, sonicate immediately prior to use. Refer to the Neurodegenerative Protein Handling Instructions on our website, or the product datasheet for further information.

1. Fairhead & Howarth. 2015. Site-specific biotinylation of purified proteins using BirA. Methods in Molecular Biology. DOI: 1007/978-1-4939-2272-7_12 2. 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.2022.05.008 3. 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.