Assays to measure PTEN lipid phosphatase activity in vitro from purified enzyme or immunoprecipitates

Laura Spinelli, Nicholas R. Leslie (Lead / Corresponding author)

Research output: Chapter in Book/Report/Conference proceedingChapter (peer-reviewed)peer-review

1 Citation (Scopus)


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.

Original languageEnglish
Title of host publicationProtein tyrosine phosphatases
Subtitle of host publicationmethods and protocols
EditorsRafael Pulido
Place of PublicationNew York
Number of pages11
ISBN (Electronic)9781493937462
ISBN (Print)9781493937448
Publication statusPublished - 2016

Publication series

NameMethods in molecular biology
ISSN (Print)1064-3745


  • Journal article
  • PTEN
  • Phosphoinositide
  • Phosphatase
  • Phosphate
  • Tumor suppressor
  • PI3-Kinase
  • Cancer


Dive into the research topics of 'Assays to measure PTEN lipid phosphatase activity in vitro from purified enzyme or immunoprecipitates'. Together they form a unique fingerprint.

Cite this