A synthetic phospho-peptide corresponding to residues surrounding Thr180 and Tyr182 of human p38 MAPK was used as immunogen. The antibody only detects p38 MAPK phosphorylated on Threonine 180 and Tyrosine 182.
Buffer
50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.
p38 MAP kinase is a mitogen-activated protein kinase that functions in various intracellular signaling cascades controlling cellular stress responses. p38 MAP kinase is activated by a variety of cellular stresses including osmotic shock, inflammatory cytokines, lipopolysaccharides (LPS), UV light and growth factors (1-3). MKK3 and SEK activate p38 MAP kinase by phosphorylation at adjacent threonine and tyrosine residues, Thr180 and Tyr182 (3,4). Activated p38 MAP kinase phosphorylates numerous downstream targets, including transcription factor ATF-2 (4).
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Western blot analysis on HeLa cell lysate using anti-Phospho-p38 MAPK (ERK1) (pT180/pY182); dilution 1:1,000. Cells were either (1) untreated, or (2) treated with Anisomycin.
