PE Mouse Anti-p38 MAPK (pT180/pY182)(36/p38 (pT180/pY182))

PE

p38 MAPK (pT180/pY182)

Mouse IgG1, κ

Phosphorylated Human p38 MAPK (pT180/pY182) Peptide

Activation of the immune and inflammatory responses often involves the recognition of bacterial endotoxin (lipopolysaccharide or LPS).  Binding of LPS by monocytes results in the production and release of proinflammatory cytokines, such as IL-1 and TNF.  LPS-induced signaling cascades involve members of the Ser/Thr protein kinase family known as the M itogen A ctivated P rotein K inases (MAPKs).  MAPK signal transduction pathways mediate the effects of various extracellular stimuli on biological processes such as proliferation, differentiation, and death.  The p38 MAPKs include p38α (MAPK14), β (MAPK11), γ (MAPK12), and δ (MAPK13).  These Ser/Thr kinases are activated by dual phosphorylation on threonine (T) and tyrosine (Y) within the motif Thr-Gly-Tyr located in kinase subdomain VIII.  Activation of p38 MAPK is mediated specifically by the M AP K inase K inases, MKK3, MKK4, and MKK6.  This leads to the activation of multiple transcription factors (NF-κB, ATF-2, Elk-1, and CHOP) that induce expression of many different genes, including proinflammatory cytokine genes.  Thus, p38 MAPKs are central kinases in multiple signal transduction pathways. The 36/p38 (pT180/pY182) monoclonal antibody recognizes the conserved dual phosphorylated site pT180/pY182 of p38α, β, γ, and δ.

Activation of the immune and inflammatory responses often involves the recognition of bacterial endotoxin (lipopolysaccharide or LPS).  Binding of LPS by monocytes results in the production and release of proinflammatory cytokines, such as IL-1 and TNF.  LPS-induced signaling cascades involve members of the Ser/Thr protein kinase family known as the M itogen A ctivated P rotein K inases (MAPKs).  MAPK signal transduction pathways mediate the effects of various extracellular stimuli on biological processes such as proliferation, differentiation, and death.  The p38 MAPKs include p38α (MAPK14), β (MAPK11), γ (MAPK12), and δ (MAPK13).  These Ser/Thr kinases are activated by dual phosphorylation on threonine (T) and tyrosine (Y) within the motif Thr-Gly-Tyr located in kinase subdomain VIII.  Activation of p38 MAPK is mediated specifically by the M AP K inase K inases, MKK3, MKK4, and MKK6.  This leads to the activation of multiple transcription factors (NF-κB, ATF-2, Elk-1, and CHOP) that induce expression of many different genes, including proinflammatory cytokine genes.  Thus, p38 MAPKs are central kinases in multiple signal transduction pathways. The 36/p38 (pT180/pY182) monoclonal antibody recognizes the conserved dual phosphorylated site pT180/pY182 of p38α, β, γ, and δ.

Mouse IgG1, κ

36/p38 (pT180/pY182)

Intracellular staining (flow cytometry) (Routinely Tested)

20 µl

Human (QC Testing)

MAPK14; p38 MAP kinase; p38 MAPK; RK; CSBP2

Phosphate

Aqueous buffered solution containing BSA and ≤0.09% sodium azide.

研发参考(3) 1. Brunet A, Pouyssegur J. Identification of MAP kinase domains by redirecting stress signals into growth factor responses. Science. 1996; 272(5268):1652-1655. (Biology). 2. Han J, Lee JD, Bibbs L, Ulevitch RJ. A MAP kinase targeted by endotoxin and hyperosmolarity in mammalian cells. Science. 1994; 265(5173):808-811. (Biology). 3. Winston BW, Chan ED, Johnson GL, Riches DW. Activation of p38mapk, MKK3, and MKK4 by TNF-alpha in mouse bone marrow-derived macrophages. J Immunol. 1997; 159(9):4491-4497. (Biology).