Unit

UNIT 18.16 Analysis of Protein Tyrosine Phosphatases and Substrates

  1. Fatih Mercan,
  2. Anton M. Bennett

Published Online: 1 JUL 2010

DOI: 10.1002/0471142727.mb1816s91

Current Protocols in Molecular Biology

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.

Author Information

  1. Yale University School of Medicine, New Haven, Connecticut

Publication History

  1. Published Online: 1 JUL 2010
  2. Published Print: JUL 2010

Abstract

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.

Keywords:

  • protein tyrosine phosphatase;
  • p-nitrophenyl phosphate;
  • malachite green;
  • in-gel phosphatase assay;
  • PTP substrates;
  • substrate-trapping