Phospho-ERK1/2 (Thr202 + Tyr204) Polyclonal Antibody

ERK1 and ERK2 are widely expressed and are involved in the regulation of meiosis, mitosis, and postmitotic functions in differentiated cells. Many different stimuli, including growth factors, cytokines, virus infection, ligands for heterotrimeric guanine nucleotidebinding 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.

ERK1; ERT2; ERK-1; PRKM3; P44ERK1; P44MAPK; HS44KDAP; HUMKER1A; p44-ERK1; p44-MAPK; Mitogen-activated protein kinase 3; MAP kinase 3; MAPK 3; Extracellular signal-regulated kinase 1; Insulin-stimulated MAP2 kinase; MAP kinase isoform p44; Microtubule-associated protein 2 kinase; MAPK3