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 language | English |
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Pages (from-to) | 292-296 |
Number of pages | 5 |
Journal | FEBS Letters |
Volume | 408 |
Issue number | 3 |
DOIs | |
Publication status | Published - 26 May 1997 |
All Science Journal Classification (ASJC) codes
- Genetics
- Molecular Biology
- Biophysics
- Structural Biology
- Biochemistry
- Cell Biology