ERK2: Monoclonal ERK2 Antibody (38H10)

Background: The mitogen-activated protein kinases (MAP kinases) play a central role in signaling pathways initiated by extracellular stimuli such as growth factors, cytokines, and various forms of environmental stress¹. To date, four major discrete groups of MAP kinases have been identified in mammalian cells, known as the extracellular signal-regulated kinases (ERK1 and ERK2), the c-Jun amino-terminal kinases (JNK1, JNK2 and JNK3), the p38 kinases (p38α, p38β, p38γ and p38δ) and ERK5/Big MAP kinase 1 (BMK1). MAP kinases are part of a three-tiered cascade consisting of a MAP kinase, a MAP kinase kinase (MAPKK, MKK or MEK) and a MAP kinase kinase kinase (MAPKKK or MEKK). Phosphorylation of the threonine and tyrosine residues in the T-loop of the MAP kinase, by its upstream kinase, results in activation. The activation of MAP kinases is not a simple switch, however, as both the duration and magnitude of activation is crucial in determining the physiological outcome in cells. Thus, it seems likely that dephosphorylation of the MAP kinases is vital for their control². These kinases have a diverse array of substrates with important functions that result in their substantial regulatory impact. The ERK/MAP kinase cascade displays not only downstream but also upstream interactions as well as cross talk with other signaling pathways, which fine-tunes the cascade in a cell type-specific fashion. Transforming agents utilize this cascade in inducing cell proliferation³.

References:

1. Cobb, M.H.: Semin Cancer Biol. 5:261, 1994.

2. Theodosiou, A. & Ashworth, A.: Genome Biology 3:1, 2002.

3. Girault, J. A. et al.: Curr Opin Pharmacol. 7:77, 2007.