p38a/SAPK2 Human

p38a, also known as Stress-Activated Protein Kinase 2 (SAPK2), is a member of the p38 MAPK family. This family of kinases plays a crucial role in cellular responses to stress and inflammation. The p38 MAPK pathway is highly conserved across species and is involved in converting extracellular stimuli into a wide range of cellular responses .

p38a/SAPK2 is a non-glycosylated polypeptide with a molecular mass of approximately 42.7 kDa . It is produced by phosphorylation of the purified p38 alpha with MKK6. The protein is relatively inactive in its non-phosphorylated form and becomes rapidly activated by dual phosphorylation of a Thr-Gly-Tyr motif .

The p38 MAPK pathway, including p38a/SAPK2, is known for its role in transducing stress signals from the environment. It regulates various cellular activities, including inflammation, cell differentiation, and apoptosis . When cells are exposed to stressors such as tumor necrosis factor, interleukin-1, or heat shock, the activation of MAPK kinase-3/6 occurs by phosphorylation. This, in turn, phosphorylates each residue of Thr180 and Tyr182 in p38 MAPK, leading to its activation .

Human recombinant p38a/SAPK2 proteins are widely used in kinase assays and other research applications. These proteins are typically expressed in E. coli and are available in various product grades . The p38 MAPK pathway has been extensively studied for its role in cancer, with p38a/SAPK2 functioning both as a tumor suppressor and a tumor promoter . This dual nature has led to the development of specific inhibitors that are being explored as potential cancer therapies .