p38 MAPK Antibody (Bi-Phospho-Thr180/Tyr182)

Polyclonal Antibody

Wet Ice

Working Dilutions:
Dot Blot: 1:1000
Western Blot: 1:1000
IHC: 1:250

Liquid. 100 ul in 10 mM HEPES (pH 7.5), 150 mM NaCl, 100 ug per ml BSA and 50% glycerol. Adequate amount of material to conduct 10-mini Western Blots.

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).

Polyclonal

Phosphopeptide corresponding to amino acid residues surrounding the phospho-Thr180 and phospho-Tyr182 of rat p38 MAPK.

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 preadsorption of the antibody with the phosphopeptide used as antigen but not by the corresponding dephosphopeptide. Human, mouse and rat have 100% amino acid sequence identity with the antigen used to raise the antibody.