ERK1/2 Monoclonal Antibody (5AD13MA), eFluor™ 570, eBioscience™, Invitrogen™

Description

• The 5AD13MA MAb recognizes human, mouse, and rat extracellular signal-regulated kinases 1 and 2 (also known as ERK1/2, p44/42, or MAPK3/1)
• ERK1/2 belong to a family of conserved serine/threonine protein kinases known as mitogen-activated protein kinases (MAPKs) that are involved in many cellular programs such as proliferation, differentiation, motility, and survival
• The ERK1/2 signaling pathway can be activated in response to a diverse range of extracellular stimuli including mitogens, growth factors, and cytokines
• The primary activators of ERK1/2 are MEK1 and MEK2 which activate p44 and p42 through phosphorylation of activation loop residues Thr202/Tyr204 and Thr185/Tyr187 in ERK1 and ERK2, respectively
• Several downstream targets of ERK1/2 have been identified, including p90RSK and the transcription factor Elk-1
• ERK1/2 are negatively regulated by MAPK phosphatases as well as by chemical inhibitors of MEK including U0126 and PD98059
• The ERK pathway is disrupted in many types of cancer and thus is an important target for diagnosis and treatment
• 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 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.