Phospho-p38 alpha (T180/Y182) Surveyor IC
Phospho-p38 alpha (T180/Y182) Surveyor IC Summary
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Background: p38 alpha
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.
Citations for Phospho-p38 alpha (T180/Y182) Surveyor IC
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
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Immunomodulation of nasal epithelial cells by Staphylococcus aureus-derived serine proteases.
Authors: Rudack C, Sachse F, Albert N, Becker K, von Eiff C
J. Immunol., 2009-11-16;183(11):7592-601. 2009-11-16
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Gene transfer to interfere with TNFalpha signaling in neuropathic pain.
Authors: Hao S, Mata M, Glorioso JC, Fink DJ
Gene Ther., 2007-04-19;14(13):1010-6. 2007-04-19
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