Phospho-Erk5 (Thr218/Tyr220) Antibody detects immunoprecipitated or transfected levels of Erk5 phosphorylated at threonine 218 and tyrosine 220. This antibody cross-reacts with phosphorylated Erk1 and Erk2. It does not cross-react with phosphorylated p38 MAPK or SAPK/JNK.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Thr218/Tyr220 of human Erk5. Antibodies are purified by protein A and peptide affinity chromatography.
Background
ERK5 (Mitogen-activated protein kinase 7, Big mitogen-activated protein kinase 1) is a member of the MAPK superfamily implicated in the regulation numerous cellular processes including proliferation, differentiation and survival (1,5-7). Like other MAPK family members, ERK5 contains a canonical activation loop TEY motif (Thr218/Tyr220) which is specifically phosphorylated by MAP2K5 (MEK5) in a growth factor-dependent, Ras-independent mechanism (2-4). For example, EGF stimulation promotes ERK5 phosphorylation which induces its traslocation to the nucleus where it phosphorylates MEF2C and other transcriptional targets (2,3). ERK5 is also activated in response to granulocyte colony-stimulating factor (G-CSF) in hematopoetic progenitor cells where is promotes survival and proliferation (4). In neuronal cells, ERK5 is required for NGF-induced neurite outgrowth neuronal homeostatis and survival (11,12). ERK5 is thought to play a role in blood vessel integrity via maintainence of endothelial cell migration and barrier function (8-10). Although broadly expressed, mice lacking erk5 display numerous cardiac defects, suggesting ERK5 plays a critical role in vascular development and homeostasis (1,5).