The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
1/100 - 1/1000.
Stress-activated, pro-apoptotic kinase which, following caspase-cleavage, enters the nucleus and induces chromatin condensation followed by internucleosomal DNA fragmentation. Key component of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein MST1/MST2, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. MST1/MST2 are required to repress proliferation of mature hepatocytes, to prevent activation of facultative adult liver stem cells (oval cells), and to inhibit tumor formation (By similarity). Phosphorylates 'Ser-14' of histone H2B (H2BS14ph) during apoptosis. Phosphorylates FOXO3 upon oxidative stress, which results in its nuclear translocation and cell death initiation.
Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. STE20 subfamily. Contains 1 protein kinase domain. Contains 1 SARAH domain.
Autophosphorylated on serine and threonine residues.
Cytoplasm. Nucleus. The caspase-cleaved form cycles between the nucleus and cytoplasm.
Immunocytochemical analysis of HepG2 cells fixed in 4% paraformaldehyde for 15 mins at room temperature labeling Serine/threonine-protein kinase 4 with ab184636 at 1/500 dilution (green) and counterstained with Hoechst 33342 (blue)