ERK1 Antibodies

ERK1 is widely expressed and involved in the regulation of meiosis, mitosis, and post-mitotic functions in differentiated cells. Many different stimuli, including growth factors, cytokines, virus infection, ligands for heterotrimeric guanine nucleotide-binding protein (G protein)-coupled receptors and transforming agents, activate the ERK1 and ERK2 pathways. When growth factors bind to the receptor tyrosine kinase, Ras interacts with Raf, the serine/threonine protein kinase and activates it as well. Once actived, Raf phosphorylates serine residue in 2 further kinases, MEK1/2, which in turn phosphorylates tyrosine/threonine in extracellular-signal regulated kinase (ERK) 1/2. Upon activation, the ERKs either phosphorylate a number of cytoplasmic targets or migrate to the nucleus, where they phosphorylate and activate a number of transcription factors such as c-Fos and Elk-1. Functionally, ERK1 is involved with a signaling cascade that regulates various cellular processes such as proliferation, differentiation, and cell cycle progression in response to a variety of extracellular signals. ERK1 is activated by upstream kinases, resulting in its translocation to the nucleus where it phosphorylates nuclear targets. Alternatively spliced transcript variants encoding different protein isoforms of ERK1 have been described.