Purification notesThe antibody was affinity purified from rabbit antiserum by affinity chromatography using epitope-specific phosphopeptide. The antibody against non phosphopeptide was removed by chromatography using non phosphopeptide corresponding to the phosphorylation site.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
1/500 - 1/1000. Detects a band of approximately 53 kDa (predicted molecular weight: 53 kDa).
1/100 - 1/500.
FunctionSerine/threonine kinase which acts as a positive regulator of apoptosis. Phosphorylates histone H3 on 'Thr-11' at centromeres during mitosis. Regulates myosin light chain phosphatase through phosphorylation of MYPT1 thereby regulating the assembly of the actin cytoskeleton, cell migration, invasiveness of tumor cells, smooth muscle contraction and neurite outgrowth. Involved in the formation of promyelocytic leukemia protein nuclear body (PML-NB), one of many subnuclear domains in the eukaryotic cell nucleus, and which is involved in oncogenesis and viral infection.
Sequence similaritiesBelongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. DAP kinase subfamily. Contains 1 protein kinase domain.
Post-translational modificationsUbiquitinated. Ubiquitination mediated by the UBE2D3 E3 ligase does not lead to proteasomal degradation, but influences promyelocytic leukemia protein nuclear bodies (PML-NBs) formation in the nucleus. Autophosphorylated. Phosphorylated by ROCK1.
Cellular localizationNucleus. Cytoplasm. Nucleus > PML body. Relocates to the cytoplasm on binding PAWR where the complex appears to interact with actin filaments (By similarity). Localizes to promyelocytic leukemia protein nuclear bodies (PML-NBs). Associates to centromeres from prophase to anaphase.