Quantifying the Kinase Activities of MST1/2

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Title: Quantifying the Kinase Activities of MST1/2
Authors: O'Driscoll, Niamh A.
Matallanas, David
Permanent link: http://hdl.handle.net/10197/9877
Date: 19-Dec-2018
Online since: 2019-04-10T08:58:49Z
Abstract: 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-32P]-ATP into a substrate immobilized in a polyacrylamide gel. We also include a protocol for indirect measurement of MST1/2 activation status using immunoblotting.
Funding Details: Science Foundation Ireland
Type of material: Book Chapter
Publisher: Springer
Volume: 1893
Start page: 289
End page: 304
Copyright (published version): 2019 Springer Nature
Keywords: ImmunoprecipitationKinase assayMST1MST2Radiolabel
DOI: 10.1007/978-1-4939-8910-2_22
Language: en
Status of Item: Peer reviewed
Is part of: Hergovich, A. (ed.). The Hippo Pathway. Methods in Molecular Biology
Appears in Collections:Medicine Research Collection

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