|Detection of Human p38δ by Western Blot. Western blot shows lysates of HepG2 human hepatocellular carcinoma cell line. PVDF membrane was probed with 5 µg/mL Mouse Anti-Human p38δ Monoclonal Antibody (Catalog # MAB1519) followed by HRP-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # HAF007). For additional reference, recombinant human p38 beta, p38 gamma, p38δ, and p38 alpha (2 ng/lane) were included. A specific band for p38 delta was detected at approximately 42 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 4.|
The p38 Mitogen-activated Protein Kinases (MAPKs) are a family of four related Ser/Thr kinases activated by proinflammatory cytokines and environmental stresses. All four p38 family members, alpha, beta, gamma, and delta, are phosphorylated by MKK3 and/or MKK6 at dual Thr and Tyr positions within the phosphoacceptor sequence Thr-Gly-Tyr. Once activated, p38 phosphorylates a number of targets, including the nuclear transcription factors ATF2 and Max.
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.
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