p38 MAPK (Phospho-Thr¹⁸⁰/Tyr¹⁸²) Polyclonal Antibody

The three mitogen-activated protein kinases (MAPKs) are evolutionarily conserved protein kinases that control a vast array of cellular processes. p38 MAPK is one of these kinases and it is activated by both inflammatory cytokines and by stress.^1,2 The p38 MAPK is thought to be particularly important in diseases like asthma and autoimmunity but it also plays important roles in the stress response of the nervous system.^3,4 Like the other MAPKs, p38 is activated by a dual specificity kinase that phosphorylates Thr¹⁸⁰ and Tyr¹⁸².⁵

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1. Johnson, G.L., and Lapadat, R. Mitogen-activated protein kinase pathways mediated by ERK, JNK, and p38 protein kinases. Science 298(5600), 1911-1912 (2002).

2. Shi, Y., and Gaestel, M. In the cellular garden of forking paths: How p38 MAPKs signal for downstream assistance. Biol. Chem. 383, 1519-1536 (2002).

3. Ying, S.W., Futter, M., Rosenblum, K., et al. Brain-derived neurotrophic factor induces long-term potentiation in intact adult hippocampus: Requirement for ERK activation coupled to CREB and upregulation of Arc synthesis. J. Neurosci. 22(5), 1532-1540 (2002).

4. Philip, S., and Armstead, W.M. Differential role of PTK, ERK, and p38 MAPK in superoxide impairment of NMDA cerebrovasodilation. Brain Res. 979, 98-103 (2003).

5. Lin, A., Minden, A., Martinetto, H., et al. Identification of a dual specificity kinase that activates the Jun kinases and p38-Mpk2. Science 268, 286-290 (1995).

Glennon, E.K.K., Torrevillas, B.K., Morrissey, S.F., et al. Abscisic acid induces a transient shift in signaling that enhances NF-kB-mediated parasite killing in the midgut of Anopheles stephensi without reducing lifespan or fecundity. Parasit. Vectors 10:333, (2017).