MAPKAPK2 Protein, Human (Active, Biotinylated)

MAPKAPK2 protein is a stress-activated serine/threonine-protein kinase with a multifaceted role in cellular processes. It participates in cytokine production, endocytosis, cytoskeleton reorganization, cell migration, cell cycle control, chromatin remodeling, DNA damage response, and transcriptional regulation. Upon stress, MAPKAPK2 is phosphorylated and activated by MAP kinase p38-alpha/MAPK14, leading to the phosphorylation of various substrates. It phosphorylates serine in specific peptide sequences and targets proteins involved in diverse cellular functions. Notably, MAPKAPK2 mediates the inflammatory response by regulating the post-transcriptional aspects of tumor necrosis factor (TNF) and IL6 production. It accomplishes this by phosphorylating AU-rich element (ARE)-binding proteins, affecting mRNA stability and translation. Additionally, MAPKAPK2 plays a crucial role in the late G2/M checkpoint following DNA damage, contributing to post-transcriptional mRNA stabilization. Its involvement in the toll-like receptor signaling pathway in dendritic cells underscores its significance in immune responses. Overall, MAPKAPK2 emerges as a key player in orchestrating cellular responses to stress and various signaling pathways.