Extracellular signal-regulated protein kinases 1 and 2 (ERK1/2) are members of the mitogen-activated protein kinase (MAPK) super family that regulate cell proliferation and apoptosis. The 44 kDa ERK1 and 42 kDa ERK2 share 83% amino acid identity with higher homology in the core regions and are expressed in almost all tissues. ERK1/2 are protein-Ser/Thr kinases that participate in the Ras-Raf-MEK-ERK signal transduction cascade. Extracellular stimuli such as growth factors, mitogens, cytokines, hormones, and oxidative or heat stress can trigger signal transduction pathways that lead to ERK1/2 activation. Human MEK1/2 phosphorylates the effector MAPKs ERK1/2 on Tyr204/187 and Thr202/185 in the TEY sequence to activate its enzymatic function.
Activated ERK1/2 preferentially phosphorylate substrates containing the Ser/Thr-Pro motif, with the optimal consensus sequence identified as Pro-Xxx-Ser/Thr-Pro. The ERK1/2 proline-directed kinases phosphorylate a multitude of cytoplasmic and nuclear protein substrates including signaling effectors, protein kinases, receptors and cytoskeletal proteins. ERK1/2 can also translocate into the nucleus and phosphorylate many transcription factors. ERK1/2 phosphorylates an array of proteins involved in various processes including cell adhesion, cell cycle progression, proliferation, migration, differentiation, cell survival and metabolism. The co-ordinated variations of ERK1/2 signalling from its duration, magnitude, subcellular localization and protein interactions can determine the final outcome of cellular fate.
Anti-ERK 1/2 Antibody (crb2005025f)
Alexa Fluor® 488 Anti-ERK1/2 antibody (crb1200306e)
ERK 1 peptide (crb1200306e)