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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 wide variety of hormones and growth factors. Cell stimulation induces a signaling cascade that leads to phosphorylation of MEK (MAPK/ERK kinase) which, in turn, activates ERK via tyrosine and threonine phosphorylation. Structural analysis of ERK2 indicates that phosphorylation induces a conformational change that exposes the active site for substrate binding. Myriad proteins represent the downstream effectors for the active ERK and implicate it in the control of cell proliferation and differentiation, as well as regulation of the cytoskeleton. Activation of ERK is normally transient and cells possess dual specificity phosphatases that are responsible for its down-regulation. Furthermore, multiple studies have shown that elevated ERK activity is associated with some cancers. ERK2 is the 42kDa member of the ERK family and is highly homologous to ERK1.Host Species: MouseClone: 33Isotype: IgG2bSpecies Reactivity: RatImmunogen: Rat ERK2 aa. 219-358Formula Weight [Chemical]: 42kDaImmunofluorescence, Immunohistochemistry, Immunoprecipitation, Western Blotting
