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Characterization of an anti-FLAG antibody binding protein in V. cholerae.
Metadata
Journalbiochemical and biophysical research communications2.985Date
2020 Jun 03
4 months ago
Type
Journal Article
Volume
2020-Jul-30 / 528 : 493-498
Author
Shin JH 1, Lanz M 2, Smolka MB 2, Dörr T 3
Affiliation
  • 2. Weill Institute for Cell and Molecular Biology, Cornell, University, Ithaca, NY, 14853, USA; Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY, 14853, USA.
  • 3. Weill Institute for Cell and Molecular Biology, Cornell, University, Ithaca, NY, 14853, USA; Department of Microbiology, Cornell University, Ithaca, NY, 14853, USA; Cornell Institute of Host-Microbe Interactions and Disease, Cornell University, Ithaca, NY, 14853, USA. Electronic address: [email protected]u.
Doi
PMIDMESH
Abstract
FLAG-tags are commonly used for protein abundance measurements and for identification of protein-protein interactions in living cells. We have observed that the cholera pathogen Vibrio cholerae encodes a FLAG-antibody-reactive protein and identified this protein as an outer membrane porin, Porin4, which contains a sequence very similar to the 3xFLAG epitope tag. We have demonstrated the binding affinity of the conserved peptide sequence (called Porin 4 tag) in Porin4 against monoclonal anti-FLAG M2 antibody. In addition, we created a porin4 deletion mutant, which can be used for background-less FLAG antibody detection experiments.
Keywords: 3xFLAG tag Affinity tag Epitope tag Monoclonal anti-FLAG M2 antibody and Porin4 Non-specific binding
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Biochem Biophys Res Communbiochemical and biophysical research communications
Metadata
LocationUnited States
FromACADEMIC PRESS INC ELSEVIER SCIENCE

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