MAPKAP kinase 2 (MK2), a serine/threonine protein kinase, is a downstream effector of the p38 mitogen-activated protein kinase (MAPK) pathway, which plays a critical role in cellular responses to stress, cytokines, and growth factors. Activated by p38α via phosphorylation at Thr334. MK2 regulates diverse processes, including mRNA stability, cytoskeletal reorganization, and inflammatory signaling. It is involved in phosphorylating substrates such as heat shock protein 27 (HSP27), cyclic AMP-responsive element-binding protein (CREB), and tristetraprolin (TTP), influencing cell survival, cytokine production, and stress adaptation.
MK2 antibodies are essential tools for studying its expression, activation, and subcellular localization. They enable detection of total MK2 protein or its phosphorylated form (active state) in techniques like Western blotting, immunofluorescence, and immunohistochemistry. These antibodies are widely used in research on inflammation, cancer, and neurodegenerative diseases, as MK2 dysregulation is linked to pathological conditions, including rheumatoid arthritis, tumor progression, and ischemia-reperfusion injury. Additionally, MK2 inhibitors are explored as therapeutic agents, making its antibodies valuable for preclinical validation.
Commercial MK2 antibodies are typically raised against specific epitopes, such as the N-terminal or kinase domains, and validated for species cross-reactivity (human, mouse, rat). Proper controls, like knockout cell lines or siRNA-mediated knockdown, are recommended to confirm antibody specificity due to potential cross-reactivity with related kinases (e.g., MK3).