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HAF109). A specific band was detected for ERK5/BMK1 at approximately 115 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1." class="big_lightbox" target="_blank">
NL001) and counterstained with DAPI (blue). Specific staining was localized to cytoplasm and nuclei. View our protocol for Fluorescent ICC Staining of Cells on Coverslips." class="big_lightbox" target="_blank">
The extracellular signal-regulated kinase 5 (ERK5), also known as MAPK7 or big mitogen-activated protein kinase 1 (BMK1), is a member of the MAP kinase subfamily (1). ERK5 differs considerably from other MAPKs; it contains an unusually long carboxyl-terminal tail which might contribute to the regulation of its activity and/or localization. In response to extracellular signals, ERK5 translocates to the nucleus, where it regulates gene expression by phosphorylating, and activating different transcription factors (2). ERK5 also differs from other MAPKs in possessing a potent transcriptional activation domain which mediates protein-protein interactions with the myocyte enhancer factor 2 (MEF2) transcription factors (3). ERK5 is specifically activated by MAPK kinase 5 (MAP2K5/MEK5) and plays an important role in mammary epithelial proliferation, endothelial cell survival and normal embryonic development (4-5).