Protein kinases play critical roles in signal transduction, and their physiological activities in cellular processes are important in defining signaling pathways. Likewise, unregulated activities of protein kinases are of particular interest in understanding pathological processes such as cancer and chronic inflammatory diseases. Protein kinases often have multiple physiological substrates and cellular functions. Therefore, specific inhibitors of protein kinases are of interest in drug development. R&D Systems now offers a wide range of new recombinant active kinases that can be used in studies of their activities and inhibitors. These include members of the Src family, and kinases involved in the PI 3-kinase and MAP kinase signaling pathways.
Figure 1. The phosphorylation of inactive p38 alpha by recombinant human active MKK6 was quantified at the indicated timepoints using the Phospho-p38 alpha (T180/Y182) DuoSet IC Kinase Assay (Catalog # DYC869). The same samples were also immunoblotted (insert) with either anti-phospho-p38 MAPK polyclonal antibody (Catalog # AF869) or anti-p38 alpha monoclonal antibody (Catalog # MAB869).