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Recombinant Expression and Purification of N-Acetylated Alpha-Synuclein

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Book cover Alpha-Synuclein

Part of the book series: Methods in Molecular Biology ((MIMB,volume 1948))

Abstract

The majority of proteins in eukaryotic cells are subject to amino-terminal (Nt) acetylation. Recombinant protein expressed using prokaryotic expression systems such as E. coli would not normally be Nt-acetylated as these cells lack the appropriate N-α-terminal acetylation complex. Here we describe a simple protocol that allows the recombinant expression and purification of Nt-acetylated alpha-synuclein (aS) from E. coli.

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References

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Acknowledgments

Work in this lab is supported by the University of Kent, BBSRC, and the Royal Society.

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Authors and Affiliations

  1. Molecular Biology, School of Biosciences, University of Kent, Canterbury, Kent, UK

    Tara A. Eastwood & Daniel P. Mulvihill

Authors
  1. Tara A. Eastwood
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  2. Daniel P. Mulvihill
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Corresponding author

Correspondence to Daniel P. Mulvihill .

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Editors and Affiliations

  1. Dementia Research Institute, University College London, London, UK

    Tim Bartels

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Eastwood, T.A., Mulvihill, D.P. (2019). Recombinant Expression and Purification of N-Acetylated Alpha-Synuclein. In: Bartels, T. (eds) Alpha-Synuclein. Methods in Molecular Biology, vol 1948. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-9124-2_10

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  • DOI: https://doi.org/10.1007/978-1-4939-9124-2_10

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  • Publisher Name: Humana Press, New York, NY

  • Print ISBN: 978-1-4939-9123-5

  • Online ISBN: 978-1-4939-9124-2

  • eBook Packages: Springer Protocols

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