Specific for the ~39k p38 MAPK protein phosphorylated at Thr180/Tyr182 in Western blots of C-6 glioma cells prepared with anisomycin treatment. Immunolabeling is blocked by the phosphopeptide used as antigen but not by the corresponding dephosphopeptide. The antibody has been directly testet for reactivity in Western blot with human tissue. It is anticipated that the antibody will also react with bovine, canine, chicken, mouse, non-human primates, rat and zebra fish based on the fact that these species have 100% homology with the amino acid sequence used as antigen.
Réactivité croisée
Humain
Homologie
bovine, canine, chicken, mouse, non-human primates, rat, zebra fish
Purification
Antigen Affinity Purified from Pooled Serum
Immunogène
Synthetic phospho-peptide corresponding to amino acid residues surrounding Thr180/Tyr182 conjugated to KLH
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 (Johnson and Lapadat, 2002, Shi and Gaestel, 2002). 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 (Philip and Armstead, 2003, Ying et al., 2002). Like the other MAPKs, p38 is activated by a dual specificity kinase that phosphorylates Thr180 and Tyr182 (Lin et al., 1995). Anti-Phospho Thr180/Tyr182 p38 MAPK Western blot of HeLa cell lysates that had been treated with UV or untreated (Control) showing specific immunolabeling of the ~39k p38 MAPK protein phosphorylated at Thr180 and Tyr182 .