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Mendeley readers
Chapter title |
Assays to Measure PTEN Lipid Phosphatase Activity In Vitro from Purified Enzyme or Immunoprecipitates
|
---|---|
Chapter number | 6 |
Book title |
Protein Tyrosine Phosphatases
|
Published in |
Methods in molecular biology, January 2016
|
DOI | 10.1007/978-1-4939-3746-2_6 |
Pubmed ID | |
Book ISBNs |
978-1-4939-3744-8, 978-1-4939-3746-2
|
Authors |
Laura Spinelli, Nicholas R. Leslie, Spinelli, Laura, Leslie, Nicholas R. |
Abstract |
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. |
Mendeley readers
The data shown below were compiled from readership statistics for 9 Mendeley readers of this research output. Click here to see the associated Mendeley record.
Geographical breakdown
Country | Count | As % |
---|---|---|
Unknown | 9 | 100% |
Demographic breakdown
Readers by professional status | Count | As % |
---|---|---|
Student > Ph. D. Student | 5 | 56% |
Student > Master | 1 | 11% |
Researcher | 1 | 11% |
Unknown | 2 | 22% |
Readers by discipline | Count | As % |
---|---|---|
Biochemistry, Genetics and Molecular Biology | 5 | 56% |
Agricultural and Biological Sciences | 1 | 11% |
Psychology | 1 | 11% |
Unknown | 2 | 22% |