Biolegend, 690256, Alexa Fluor® 488 anti-p38 MAPK Phospho (Thr180/Tyr182) Recombinant Antibody

Mitogen activated protein kinases (MAPK) are a family of highly conserved intracellular kinases that transduce extracellular signals relayed by surface receptors or various types of damage. Three subfamilies exist in mammals, including ERK, JNK, and p38 kinases. Four p38 MAPK family members have been identified: p38a, p38b, p38g, and p38d. p38a is ubiquitously expressed usually at high levels, whereas p38b is expressed at lower levels. The expression patterns of p38g and p38d are more restricted. Most of the functions that are generally ascribed to p38 MAPKs refer to p38a, which is encoded by the MAPK14 gene. The p38 MAP kinase is activated by treatment of cells with proinflammatory cytokines (e.g. TNF and IL-1) or by exposure of cells to environmental stress (e.g. UV radiation and osmotic shock). This activation results in the phosphorylation of residues Thr180 and Tyr182. Over 100 proteins can be directly phosphorylated by p38a and a significant proportion of them are involved in the regulation of gene expression. In addition, the p38a pathway can control at different levels the production of extracellular signaling molecules, such as cytokines, chemokines, and growth factors. The p38a signaling pathway has dual roles in tumorigenesis. During oncogene-induced tumor initiation and in the early response to carcinogens, p38a mainly acts as a tumor suppressor by maintaining cell homeostasis and eventually inducing cell death. However, p38a function is sometimes altered in the tumor cell so that it favors tumor progression. This might be due to changes in gene expression programs that accompany malignant cell transformation or could be driven by different stimuli available in the microenvironment.