Search by product name, CAS, target or catalog number. Press Down Arrow to reach product suggestions, Tab to move between links, and Escape to close suggestions.
Extracellular signal-regulated kinase (ERK) inhibitors act on ERK1 and ERK2 at the end of a growth factor cascade. ERK1 and ERK2 were described in 1991 as kinases activated and tyrosine phosphorylated in response to insulin and nerve growth factor. Mitogen-activated protein kinase kinases (MEK1, MEK2) activate them, and they phosphorylate many cytoplasmic and nuclear substrates. SCH772984, reported in 2013, inhibits ERK1 and ERK2 in models of acquired resistance to B-Raf and MEK1/2 inhibitors. Ulixertinib and FR 180204 are further ERK1/2 inhibitors, whereas XMD8-92 targets ERK5, also called big mitogen-activated protein kinase 1 (BMK1). The list also holds compounds with an indirect link to the pathway, such as the plant cytokinin trans-zeatin.
PPM-3 is a potent and selective PROTAC degrader of ERK5, exhibiting an IC50 of 62.4 nM. While PPM-3 does not directly affect tumor cell proliferation, it modulates tumor development by impacting macrophage differentiation. This compound may serve as a valuable tool for investigating the role of ERK5 degradation in cancer biology and immune modulation.
PROTAC ERK5 degrader-1 is a bifunctional compound designed to target and induce degradation of ERK5 through the VHL-mediated proteasome pathway. Its biological activity has been demonstrated in MOLT-4 cells, highlighting its potential utility in research focused on diseases characterized by dysregulated ERK5 activity, such as acute lymphoblastic leukemia. This reagent is suitable for studies aimed at elucidating the role of ERK5 in various pathophysiological contexts.
