Membrane Protein Production in Escherichia coli.


Journal

Methods in molecular biology (Clifton, N.J.)
ISSN: 1940-6029
Titre abrégé: Methods Mol Biol
Pays: United States
ID NLM: 9214969

Informations de publication

Date de publication:
2020
Historique:
entrez: 1 3 2020
pubmed: 1 3 2020
medline: 9 3 2021
Statut: ppublish

Résumé

Escherichia coli is the workhorse of the structural biology lab. In addition to routine cloning and molecular biology, E. coli can be used as a factory for the production of recombinant membrane proteins. Purification of homogeneous samples of membrane protein expressed in E. coli is a significant bottleneck for researchers, and the protocol we present here for the overexpression and purification of membrane proteins in E. coli will provide a solid basis to develop lab- and protein-specific protocols for your membrane protein of interest. We additionally provide extensive notes on the purification process, as well as the theory surrounding principles of purification.

Identifiants

pubmed: 32112312
doi: 10.1007/978-1-0716-0373-4_2
doi:

Substances chimiques

Membrane Proteins 0
Membrane Transport Proteins 0
Recombinant Fusion Proteins 0
Recombinant Proteins 0

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

13-27

Auteurs

Benjamin C McIlwain (BC)

Department of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI, USA. mcilwain@umich.edu.

Ali A Kermani (AA)

Department of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI, USA. kermania@umich.edu.

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Classifications MeSH