Detection of ERK activation by a novel monoclonal antibody

Y Yung, Y Dolginov, Zhong Yao, H Rubinfeld, Dan Yosef Michael, Tamar Hanoch, E Roubini, Z Lando, D Zharhary, Rony Seger

Research output: Contribution to journalArticlepeer-review

114 Citations (Scopus)

Abstract

The mitogen-activated protein kinase, ERK is activated by a dual phosphorylation on threonine and tyrosine residues. Using a synthetic diphospho peptide, we have generated a monoclonal antibody directed to the active ERK. The antibody specifically identified the active doubly phosphorylated, but not the inactive mono- or non-phosphorylated forms of ERKs. A direct correlation was observed between ERK activity and the intensity in Western blot of mitogen-activated protein kinases from several species. The antibody was proven suitable for immunofluorescence staining, revealing a transient reactivity with ERKs that were translocated to the nucleus upon stimulation. In conclusion, the antibody can serve as a useful tool in the study of ERK signaling in a wide variety of organisms.

Original languageEnglish
Pages (from-to)292-296
Number of pages5
JournalFEBS Letters
Volume408
Issue number3
DOIs
Publication statusPublished - 26 May 1997

All Science Journal Classification (ASJC) codes

  • Genetics
  • Molecular Biology
  • Biophysics
  • Structural Biology
  • Biochemistry
  • Cell Biology

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