Activation of the immune and inflammatory responses often involves the recognition of bacterial endotoxin (lipopolysaccharide or LPS). Binding of LPS by monocytic cells results in the production and release of proinflammatory cytokines, such as IL-1 and TNF-α. LPS-induced signaling cascades involve members of the Ser/Thr protein kinase family known as the mitogen activated protein kinases (MAPKs). One of these, p38 MAP kinase (p38 MAPK or CSPB2), is a human homologue of HOG1, a yeast MAP kinase that is essential for growth under conditions of elevated osmolarity. Similar to HOG1, p38 MAPK is phosphorylated in response to hyperosmolarity, but also in response to a variety of stimuli including LPS, IL-1, or TNF-α. Efficient activation of p38 MAPK requires phosphorylation of Thr-180 and Tyr-182. At least three Thr/Tyr kinases (MKK3, MKK4/SEK1, and MKK6) phosphorylate and activate p38 MAPK. This leads to the activation of multiple transcription factors (NF-κB, ATF-2, Elk-1, and CHOP/GADD143) that induce expression of proinflammatory cytokine genes. In addition to its role in immunity, p38 MAPK is widely expressed and serves as an important signal transducer in a variety of cell types.
This antibody is routinely tested by western blot analysis. Other applications were tested at BD Biosciences Pharmingen during antibody development only or reported in the literature.