p38 alpha-MAPK14

The p38 Mitogen-activated Protein Kinases (MAPKs) are a family of four related Ser/Thr kinases activated by proinflammatory cytokines and environmental stresses.

The most frequently analyzed family member, p38 alpha, also known as SAPK2a and MAPK14, was initially purified as a kinase critical to the signaling cascade linking IL-1 to MAPKAPK-2 and the small heat shock protein HSP27. Ubiquitously expressed, p38 alpha is dually phosphorylated by MKK3 and MKK6 at Thr180 and Tyr182. Once activated, p38 alpha phosphorylates a number of targets, including the cytoplasmic kinases MNK 4 and PRAK5 and the nuclear transcription factors ATF2 1 and STAT1. Several promising compounds that inhibit p38 alpha are being investigated as potential therapies for arthritic and inflammatory diseases.

Image: Orexin B and p38 alpha  were detected in frozen sections of mouse brainstem using mouse anti-human Orexin B monoclonal antibody (red) and rabbit anti-human/mouse/rat p38 alpha affinity-purified polyclonal antibody (green).

Image: Detection of p38α by western blotting. Human HeLa cells, mouse NIH/3T3 cells, and rat PC12 cells were solubilized in SDS sample buffer and extract from 2 x 10⁵cells was loaded in each lane. Extracts were run on a 12% polyacrylamide gel, transferred to Immobilon membrane, and immunoblotted with 0.25 μg/mL rabbit anti-p38α, as described in Datasheet. A 5 second exposure to film is shown.