Exploiting Ligand-Protein Conjugates to Monitor Ligand-Receptor Interactions

We introduce three assays for analyzing ligand-receptor interactions based on the specific conjugation of ligands to SNAP-tag fusion proteins. Conjugation of ligands to different SNAP-tag fusions permits the validation of suspected interactions in cell extracts and fixed cells as well as the establi...

Descripción completa

Detalles Bibliográficos
Autores principales: Haruki, Hirohito, Gonzalez, Monica Rengifo, Johnsson, Kai
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2012
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3365113/
https://www.ncbi.nlm.nih.gov/pubmed/22701522
http://dx.doi.org/10.1371/journal.pone.0037598
_version_ 1782234644115095552
author Haruki, Hirohito
Gonzalez, Monica Rengifo
Johnsson, Kai
author_facet Haruki, Hirohito
Gonzalez, Monica Rengifo
Johnsson, Kai
author_sort Haruki, Hirohito
collection PubMed
description We introduce three assays for analyzing ligand-receptor interactions based on the specific conjugation of ligands to SNAP-tag fusion proteins. Conjugation of ligands to different SNAP-tag fusions permits the validation of suspected interactions in cell extracts and fixed cells as well as the establishment of high-throughput assays. The different assays allow the analysis of strong and weak interactions. Conversion of ligands into SNAP-tag substrates thus provides access to a powerful toolbox for the analysis of their interactions with proteins.
format Online
Article
Text
id pubmed-3365113
institution National Center for Biotechnology Information
language English
publishDate 2012
publisher Public Library of Science
record_format MEDLINE/PubMed
spelling pubmed-33651132012-06-14 Exploiting Ligand-Protein Conjugates to Monitor Ligand-Receptor Interactions Haruki, Hirohito Gonzalez, Monica Rengifo Johnsson, Kai PLoS One Research Article We introduce three assays for analyzing ligand-receptor interactions based on the specific conjugation of ligands to SNAP-tag fusion proteins. Conjugation of ligands to different SNAP-tag fusions permits the validation of suspected interactions in cell extracts and fixed cells as well as the establishment of high-throughput assays. The different assays allow the analysis of strong and weak interactions. Conversion of ligands into SNAP-tag substrates thus provides access to a powerful toolbox for the analysis of their interactions with proteins. Public Library of Science 2012-05-31 /pmc/articles/PMC3365113/ /pubmed/22701522 http://dx.doi.org/10.1371/journal.pone.0037598 Text en Haruki et al. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Haruki, Hirohito
Gonzalez, Monica Rengifo
Johnsson, Kai
Exploiting Ligand-Protein Conjugates to Monitor Ligand-Receptor Interactions
title Exploiting Ligand-Protein Conjugates to Monitor Ligand-Receptor Interactions
title_full Exploiting Ligand-Protein Conjugates to Monitor Ligand-Receptor Interactions
title_fullStr Exploiting Ligand-Protein Conjugates to Monitor Ligand-Receptor Interactions
title_full_unstemmed Exploiting Ligand-Protein Conjugates to Monitor Ligand-Receptor Interactions
title_short Exploiting Ligand-Protein Conjugates to Monitor Ligand-Receptor Interactions
title_sort exploiting ligand-protein conjugates to monitor ligand-receptor interactions
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3365113/
https://www.ncbi.nlm.nih.gov/pubmed/22701522
http://dx.doi.org/10.1371/journal.pone.0037598
work_keys_str_mv AT harukihirohito exploitingligandproteinconjugatestomonitorligandreceptorinteractions
AT gonzalezmonicarengifo exploitingligandproteinconjugatestomonitorligandreceptorinteractions
AT johnssonkai exploitingligandproteinconjugatestomonitorligandreceptorinteractions

Ejemplares similares