Detection of ERK activation by a novel monoclonal antibody

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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.

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