Quantifying the Kinase Activities of MST1/2.


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:
2019
Historique:
entrez: 20 12 2018
pubmed: 20 12 2018
medline: 7 6 2019
Statut: ppublish

Résumé

The functions of the kinases MST1 and MST2 rely heavily on their ability to phosphorylate and become phosphorylated themselves. Hence, it is important to precisely measure the kinase activities of both isoforms in a reproducible manner. Here, we describe in detail the protocol for an in-gel kinase assay for the quantification of the kinase activity of MST1/2, which involves immunoprecipitation of MST1/2 and the incorporation of radiolabeled phosphate from [γ-

Identifiants

pubmed: 30565142
doi: 10.1007/978-1-4939-8910-2_22
doi:

Substances chimiques

Protein Serine-Threonine Kinases EC 2.7.11.1

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

289-304

Auteurs

Niamh A O'Driscoll (NA)

Systems Biology Ireland, University College Dublin, Belfield, Dublin, Ireland.
School of Medicine, University College Dublin, Belfield, Dublin, Ireland.

David Matallanas (D)

Systems Biology Ireland, University College Dublin, Belfield, Dublin, Ireland. david.gomez@ucd.ie.
School of Medicine, University College Dublin, Belfield, Dublin, Ireland. david.gomez@ucd.ie.

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Classifications MeSH