p38 alpha/MAPK14 Protein, Human (Active, sf9, His)

p38 alpha/MAPK14, a serine/threonine kinase integral to the MAP kinase signal transduction pathway, is among the four p38 MAPKs crucial for cellular responses to extracellular stimuli such as pro-inflammatory cytokines or physical stress, resulting in the direct activation of transcription factors. In this cascade, p38 MAPKs phosphorylate a diverse range of proteins, estimated at approximately 200 to 300 substrates each. These include downstream kinases like RPS6KA5/MSK1 and RPS6KA4/MSK2, which directly phosphorylate and activate transcription factors and histone H3, playing pivotal roles in the rapid induction of immediate-early genes in response to stress or mitogenic stimuli. Additionally, p38 MAPK14 regulates protein translation, impacts cytoskeletal remodeling, and participates in various cellular processes such as endosomal dynamics, protein turnover, and ectodomain shedding of transmembrane proteins. In the nucleus, it phosphorylates and activates transcription factors involved in the inflammatory response, modulating gene expression and chromatin dynamics. Furthermore, p38 MAPK14 is implicated in diverse cellular functions, including the regulation of glucose uptake, skin development, and erythropoiesis, and exhibits kinase-independent roles, such as the regulation of O-Glc-N-acylation. Its activation by phosphorylation in response to UV-B irradiation and ribosome collisions contributes to the NLRP1 inflammasome activation and pyroptosis. Additionally, during microbial infection, p38 alpha/MAPK14 is activated by phosphorylation, inhibiting IFN-gamma production in T-cells.