Alexa FluorTM 488 Mouse anti-Rat, Ms, Hu BD™ Phosflow ERK1/2 (pT202/pY204) by BD Biosciences

The family of serine/threonine kinases known as ERKs (extracellular signal regulated kinases) or MAPKs (mitogen-activated protein kinases) are activated after cell stimulation by a variety of hormones and growth factors. A myriad of proteins, such as kinases, phosphatases, transcription factors, and cytoskeletal proteins, are substrates for the active ERK. These proteins implicate ERK function in the control of cell proliferation and differentiation, as well as in the regulation of the cytoskeleton. Activation of ERK is normally transient and cells possess dual specificity phosphatases that are responsible for
its down-regulation. ERK1 is a 44 kDa member of the ERK family and shares 85% homology with ERK2. In rat, these proteins are phosphorylated at T202/Y204 and T183/Y185, respectively. ERK1 and 2 have been implicated in growth factor signaling, as well as other signal transduction pathways. Growth factor stimulation leads to activation of Ras and Raf, leading to phosphorylation of MEK1 (MAPK/ERK kinase) which, in turn, activates ERK via dual phosphorylation. Thus, ERK1 and 2 are critical kinases in multiple
signal transduction pathways that regulate cell growth and differentiation.