Recombinant Human MST2/STK3 Protein was resolved with SDS-PAGE under reducing (Lane 1) and non-reducing (Lane 2) conditions.
The activity of MST2 is based on the MSA technology, and the content and ratio of the substrate and the product are directly separated and detected in real time and dynamically by the different migration rates of the substrate and the product after the enzymatic reaction.
Human serine/threonine-protein kinase 3 (STK3, or MST2) is a 56,301 Da monomer with three domains: a SARAH domain, composed of a long α-helix at the C-terminus that when dimerized, forms an antiparallel dimeric coiled-coil, an inhibitory domain, and a catalytic kinase domain at the N-terminus. STK3 is activated through autophosphorylation by dimerizing with itself or heterodimerizing with its homolog, MST1 (STK4). In addition to activation by straurosporine and FAS ligand, STK3 has been found to be activated through dissociation of GLRX and Thioredoxin (Trx1) from STK3 under oxidative stress. In many types of cancers, the proto-oncogene c-Raf binds to the SARAH domain of MST2 and prevents RASSF1A-mediated MST2 dimerization and subsequent downstream pro-apoptotic signaling.
