p38 delta/MAPK13 Protein, Human (Active, sf9, GST)

p38 delta/MAPK13, a serine/threonine kinase and integral component of the MAP kinase signal transduction pathway, is among the four p38 MAPKs pivotal in orchestrating cellular responses triggered by extracellular stimuli like pro-inflammatory cytokines or physical stress, resulting in the direct activation of transcription factors such as ELK1 and ATF2. Operating within this cascade, p38 MAPKs phosphorylate an extensive array of proteins, estimated at approximately 200 to 300 substrates each, with MAPK13 representing one of the less studied isoforms. It targets downstream kinases like MAPKAPK2, activating them through phosphorylation to further impact additional substrates. MAPK13 plays a critical role in regulating protein translation by phosphorylating and inactivating EEF2K, contributing to cytoskeletal remodeling through the phosphorylation of MAPT and STMN1. Moreover, it mediates UV irradiation-induced up-regulation of the gene expression of CXCL14 and plays a vital role in the regulation of epidermal keratinocyte differentiation, apoptosis, and skin tumor development. In response to stress, MAPK13 phosphorylates the transcriptional activator MYB, leading to rapid MYB degradation via a proteasome-dependent pathway. Additionally, MAPK13 phosphorylates and down-regulates PRKD1 during the regulation of insulin secretion in pancreatic beta cells.