MNK2 (MAP kinase-interacting kinase 2) contains a conserved C-terminal ERK-interacting domain, a catalytic domain with homology to the calcium/calmodulin-dependent family of kinases, and putative MAP kinase phosphorylation sites located within the T loop of the kinase domain. MNK2 binds tightly to the growth factor-regulated MAP kinases, ERK1 and ERK2. ERK and p38 phosphorylate MNK2, which stimulates its in vitro kinase activity toward a substrate, eukaryotic initiation factor-4E (eIF-4E).A yeast two-hybrid screen showed the MNK2 protein interacted with the ligand-binding domain of estrogen receptor beta (ERbeta).
Physical form
Supplied in 50 mM Tris-HCl, pH 7.5, with 150 mM NaCl, 0.2 5mM DTT, 0.1 mM EGTA, 0.1 mM EDTA, 0.1 mM PMSF, and 25% glycerol.
Legal Information
PRECISIO is a registered trademark of Merck KGaA, Darmstadt, Germany
We have identified and characterized the human Mnk2 gene (HGMW-approved gene symbol MKNK2) through a yeast two-hybrid screen in which the Mnk2 protein interacted with the ligand-binding domain of estrogen receptor beta (ERbeta). Human Mnk2 is homologous to murine Mnk2
Mitogen-activated protein (MAP) kinases bind tightly to many of their physiologically relevant substrates. We have identified a new subfamily of murine serine/threonine kinases, whose members, MAP kinase-interacting kinase 1 (Mnk1) and Mnk2, bind tightly to the growth factor-regulated MAP kinases
Questions
Reviews
★★★★★ No rating value
Active Filters
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
