Spinelli Laura, Leslie Nicholas R
Institute of Biological Chemistry, Biophysics and Bioengineering, Heriot Watt University, Nasmyth Building, Riccarton Campus, Edinburgh, EH14 4AS, UK.
Division of Cell Signalling and Immunology, School of Life Sciences, University of Dundee, Dundee, UK.
Methods Mol Biol. 2016;1447:95-105. doi: 10.1007/978-1-4939-3746-2_6.
PTEN is a one of the most frequently mutated tumor suppressors in human cancers. It is essential for regulating diverse biological processes and through its lipid phosphatase activity regulates the PI 3-Kinase signaling pathway. Sensitive phosphatase assays are employed to study the catalytic activity of PTEN against phospholipid substrates. Here we describe protocols to assay PTEN lipid phosphatase activity using either purified enzyme (purified PTEN lipid phosphatase assay) or PTEN immunopurified from tissues or cultured cells (cellular IP PTEN lipid phosphatase assay) against vesicles containing radiolabeled PIP3 substrate.
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