Nonradioactive Assay of FLAG®-Tagged MAPK Using ANTI-FLAG® Antibody-Coated Multiwell Plates

We have developed a rapid, sensitive, and quantitative 96-well microplate-based nonradioactive immunoprecipitation/kinase assay to evaluate mitogen-activated protein kinase (MAPK) activity. Three quantitative nonradioactive imunoprecipitation/kinase assays of MAPK were demonstrated on a 96-well micr...

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Main Authors: L. Zhang, S. Uder, T. Juehne, B. Brizzard, K. Song
Format: Article
Language:English
Published: Taylor & Francis Group 2002-02-01
Series:BioTechniques
Online Access:https://www.future-science.com/doi/10.2144/02322pf02
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author L. Zhang
S. Uder
T. Juehne
B. Brizzard
K. Song
author_facet L. Zhang
S. Uder
T. Juehne
B. Brizzard
K. Song
author_sort L. Zhang
collection DOAJ
description We have developed a rapid, sensitive, and quantitative 96-well microplate-based nonradioactive immunoprecipitation/kinase assay to evaluate mitogen-activated protein kinase (MAPK) activity. Three quantitative nonradioactive imunoprecipitation/kinase assays of MAPK were demonstrated on a 96-well microplate coated with ANTI-FLAG® M2 antibody (ANTI-FLAG M2 plate): (i) the capture of phosphorylated FLAG®-tagged MAPK fusion protein (FLAG-MAPK) from phorbol esters-stimulated, FLAG-MAPK-transfected COS-7 cells, coupled with a very sensitive ELISA procedure to quantitate the level of phosphorylation of FLAG-MAPK; (ii) the in vitro kinase reaction of FLAG-MAPK activity with a substrate and ATP in the same well used to captured the phosphorylated FLAG-MAPK; and (iii) the in vitro kinase reaction of captured non-activated FLAG-MAPK by its upstream kinase from phorbol 12-myristate 13-acetate (PMA)-stimulated COS-7 cells. These results demonstrate that the ANTI-FLAG M2 plate allows for the rapid and quantitative determination of phosphorylation of FLAG-MAPK directly from stimulated, transfected cell lysate. Captured, phosphorylated FLAG-MAPK retains catalytic activity as demonstrated by the phosphorylation of Elk-1 in the same well. Furthermore, phosphorylation of captured FLAG-MAPK by the upstream kinases can be observed directly on the plate. These assays are sensitive, specific, and suitable for handling multiple samples. Thus, the ANTI-FLAG M2 plate forms the basis of a high-throughput screening platform in kinase analysis.
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spelling doaj-art-7e10e6cd099c46f4bb32c8ba528a9bd32025-08-20T02:25:51ZengTaylor & Francis GroupBioTechniques0736-62051940-98182002-02-0132244244710.2144/02322pf02Nonradioactive Assay of FLAG®-Tagged MAPK Using ANTI-FLAG® Antibody-Coated Multiwell PlatesL. Zhang0S. Uder1T. Juehne2B. Brizzard3K. Song41Sigma-Aldrich, St. Louis, MO, USA1Sigma-Aldrich, St. Louis, MO, USA1Sigma-Aldrich, St. Louis, MO, USA1Sigma-Aldrich, St. Louis, MO, USA1Sigma-Aldrich, St. Louis, MO, USAWe have developed a rapid, sensitive, and quantitative 96-well microplate-based nonradioactive immunoprecipitation/kinase assay to evaluate mitogen-activated protein kinase (MAPK) activity. Three quantitative nonradioactive imunoprecipitation/kinase assays of MAPK were demonstrated on a 96-well microplate coated with ANTI-FLAG® M2 antibody (ANTI-FLAG M2 plate): (i) the capture of phosphorylated FLAG®-tagged MAPK fusion protein (FLAG-MAPK) from phorbol esters-stimulated, FLAG-MAPK-transfected COS-7 cells, coupled with a very sensitive ELISA procedure to quantitate the level of phosphorylation of FLAG-MAPK; (ii) the in vitro kinase reaction of FLAG-MAPK activity with a substrate and ATP in the same well used to captured the phosphorylated FLAG-MAPK; and (iii) the in vitro kinase reaction of captured non-activated FLAG-MAPK by its upstream kinase from phorbol 12-myristate 13-acetate (PMA)-stimulated COS-7 cells. These results demonstrate that the ANTI-FLAG M2 plate allows for the rapid and quantitative determination of phosphorylation of FLAG-MAPK directly from stimulated, transfected cell lysate. Captured, phosphorylated FLAG-MAPK retains catalytic activity as demonstrated by the phosphorylation of Elk-1 in the same well. Furthermore, phosphorylation of captured FLAG-MAPK by the upstream kinases can be observed directly on the plate. These assays are sensitive, specific, and suitable for handling multiple samples. Thus, the ANTI-FLAG M2 plate forms the basis of a high-throughput screening platform in kinase analysis.https://www.future-science.com/doi/10.2144/02322pf02
spellingShingle L. Zhang
S. Uder
T. Juehne
B. Brizzard
K. Song
Nonradioactive Assay of FLAG®-Tagged MAPK Using ANTI-FLAG® Antibody-Coated Multiwell Plates
BioTechniques
title Nonradioactive Assay of FLAG®-Tagged MAPK Using ANTI-FLAG® Antibody-Coated Multiwell Plates
title_full Nonradioactive Assay of FLAG®-Tagged MAPK Using ANTI-FLAG® Antibody-Coated Multiwell Plates
title_fullStr Nonradioactive Assay of FLAG®-Tagged MAPK Using ANTI-FLAG® Antibody-Coated Multiwell Plates
title_full_unstemmed Nonradioactive Assay of FLAG®-Tagged MAPK Using ANTI-FLAG® Antibody-Coated Multiwell Plates
title_short Nonradioactive Assay of FLAG®-Tagged MAPK Using ANTI-FLAG® Antibody-Coated Multiwell Plates
title_sort nonradioactive assay of flag r tagged mapk using anti flag r antibody coated multiwell plates
url https://www.future-science.com/doi/10.2144/02322pf02
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