P38 MAPK (phospho Thr180 / Tyr182) 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 these kinases and it is activated by both inflammatory cytokines and by stress. 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. Like the other MAPKs, p38 is activated by a dual specificity kinase that phosphorylates Thr180 and Tyr182.

P38 MAPK (Thr180/Tyr182) polyclonal antibody was raised against a synthetic phosphopeptide corresponding to amino acids residues surrounding the phospho Thr180/Tyr182 of p38.

For long term storage –80˚ C is recommended, but shorter term storage at –20˚ C is also acceptable as aliquots may be taken without freeze/thawing due to the presence of 50% glycerol. Stable for one year.

Immunolabeling in Western blots of C-6 glioma cells prepared with anisomycin treatment is blocked by the phosphopeptide used as antigen but not by the corresponding dephosphopeptide. Applications include Immunoblotting (DB) and Western Blots (WB) . Immunohistochemistry (IHC) : not yet determined. Human, mouse and rat have 100% amino acid sequence identity with the antigen used to raise the antibody. When internally tested under ideal conditions the working dilutions were 1:1000 for DB and WB.

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Choe, E.S. and McGinty, J.F., "N-methyl-D-aspartate receptors and P38 mitogen-activated protein kinase are required for cAMP-dependent cyclase response element binding protein and ELK-1 phosphorylation in the striatum, " Neurosci. 101 (2000) 607 - 617.