| Stress-activated serine/threonine-protein kinase involved in cytokine production, endocytosis, reorganization of the cytoskeleton, cell migration, cell cycle control, chromatin remodeling, DNA damage response and transcriptional regulation. Following stress, it is phosphorylated and activated by MAP kinase p38-alpha/MAPK14, leading to phosphorylation of substrates. Phosphorylates serine in the peptide sequence, Hyd-X-R-X2-S, where Hyd is a large hydrophobic residue. Phosphorylates ALOX5, CDC25B, CDC25C, CEP131, ELAVL1, HNRNPA0, HSP27/HSPB1, KRT18, KRT20, LIMK1, LSP1, PABPC1, PARN, PDE4A, RCSD1, RPS6KA3, TAB3 and TTP/ZFP36. Phosphorylates HSF1, leading to the interaction with HSP90 proteins and inhibiting HSF1 homotrimerization, DNA-binding and transactivation activities (By similarity). Full length inactive recombinant protein corresponding to mouse ERK2/MAPK2, with mutation on lysine52 to arginine, fused with a N-terminal 6X -HisTag, expressed in E. coli. Swiss/Uniport: P49138 Applications: A suitable substrate of MEK1. Other applications not tested. Recommended Dilution: Optimal dilutions to be determined by the researcher. Storage and Stability: Aliquot to avoid repeated freezing and thawing and store at -70C. Aliquots are stable for 6 months after receipt. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. |
