UNIT 18.16 Analysis of Protein Tyrosine Phosphatases and Substrates
Published Online: 1 JUL 2010
Copyright © 2010 by John Wiley & Sons, Inc.
Lab Protocol Title
Current Protocols in Molecular Biology
How to Cite
Mercan, F. and Bennett, A. M. 2010. Analysis of Protein Tyrosine Phosphatases and Substrates. Current Protocols in Molecular Biology. 91:18.16:18.16.1–18.16.17.
- Published Online: 1 JUL 2010
- Published Print: JUL 2010
Protein tyrosine phosphorylation is a reversible post-translational modification that is essential for life in eukaryotic cells. The combinatorial action of both protein tyrosine kinases and protein tyrosine phosphatases (PTPs) determines the net level of cellular tyrosine phosphorylation. This unit discusses methods to determine the level of protein tyrosine phosphatase activity and methods for discovering novel substrates for protein tyrosine phosphatases. Curr. Protoc. Mol. Biol. 91:18.16.1-18.16.17. © 2010 by John Wiley & Sons, Inc.
- protein tyrosine phosphatase;
- p-nitrophenyl phosphate;
- malachite green;
- in-gel phosphatase assay;
- PTP substrates;