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J. Biol. Chem. 274, 27177-27184. c-Raf-mediated inhibition of epidermal growth factor-stimulated cell migration. 1999

Slack, J.K., Catling, A.D., Eblen, S.T., Weber, M.J., Parsons, J.T.

Notes: Pretreatment of REF52 cells for 15minutes with 50µM U0126 MEK Inhibitor prior to stimulation with EGF blocked all ERK phosphorylation. The same experiment with the PD98059 inhibitor did not block ERK phosphorylation. (0377)

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EMBO J. 18, 6973-6982. Cell type-specific activation of mitogen-activated protein kinases by CpG-DNA controls interleukin-12 release from antigen-presenting cells. 1999

Hacker, H., Mischak, H., Hacker, G., Eser, S., Prenzel, N., Ullrich, A., Wagner, H.

Notes: Treatment of RAW 264.7 cells were treated with CpG-oligonucleotides derived from bacterial DNA. The cells responded by releasing TNFα and IL-12. The MEK Inhibitor U0126 inhibited the release of the proteins. The inhibitor has no effect on the TNFα promoter or mRNA levels but has a big effect on IL-12 promoter activity and mRNA levels, suggesting different mechanisms of MAPK pathway involvement. Promoter studies were performed with constructs made in the pGL3-Basic Vector and analyzed with the Luciferase Assay System. (1091)

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J. Immunol. 163, 5786-5795. Differential role for p38 mitogen-activated protein kinase in regulating CD40-induced gene expression in dendritic cells and B cells. 1999

Aicher, A., Shu, G.L., Magaletti, D., Mulvania, T., Pezzutto, A., Craxton, A. and Clark, E.A.

Notes: The U0126 MEK Inhibitor was used to inhibit Erk phosphorylation in dendritic cells upon CD40 ligation. The U0126 Inhibitor (0.5-1µM) reduced phosphoErk2 from sevenfold to twofold. Higher concentrations completely inhibited phosphorylation. (2066)

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J. Biol. Chem. 274, 24965-24972. Leukemia inhibitory factor and its receptor promote adipocyte differentiation via the mitogen-activated protein kinase cascade. 1999

Aubert, J., Dessolin, S., Belmonte, N., Li, M., McKenzie, F.R., Staccini, L., Villageois, P., Barhanin, B., Vernallis, A., Smith, A.G., Ailhaud, G. and Dani, C.

Notes: The effect of the U0126, MEK Inhibitor is reported and compared to that of the inhibitor PD98059. PD98059 inhibited an Erk-dependent glycerol-phosphate dehydrogenase activity by 60% at 10µM. The same inhibition was seen with U0126 at 0.5µM. Also, 10µM PD98059 produced 50% inhibition of LIF-stimulated C/EBP gene expression whereas 10µM U0126 completely prevented the expression (no other concentrations of U0126 reported). (1484)

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J. Pharmacol. Exp. Ther. 291, 1179-1187. Mechanisms of 5-hydroxytryptamine-2A receptor activation of the mitogen-activated protein kinase pathway in vascular smooth muscle. 1999

Banes, A., Florian, J.A. and Watts, S.W.

Notes: This paper describes inhibition of 5-hydroxytryptamine induced aortic contraction by the MEK Inhibitor U0126. The inhibitor was tested at 20 and 50µM and both were inhibitory. Use of U0126 Inhibitor and nifedipine, a calcium channel antagonist, produced almost complete inhibition. The MEK Inhibitor U0126 also greatly inhibited KCl induced aortic contraction. The cell extracts also demonstrated that the U0126 Inhibitor blocked MAPK phosphorylation. The tissue was treated with the inhibitor for 1 hour prior to addition of the agonist. (2231)

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J. Biol. Chem. 274, 6168-6174. Nuclear localization of mitogen-activated protein kinase kinase 1 (MKK1) is promoted by serum stimulation and G2-M progression. Requirement for phosphorylation at the activation lip and signaling downstream of MKK. 1999

Tolwinski, N.S., Shapiro, P.S., Goueli, S., and Ahn, N.G.

Notes: Authors used the Anti-ERK 1/2 pAb and MEK Inhibitor U0126 to study localization of Erk1 and Erk2 in NIH 3T3 cells.  The Anti-ERK 1/2 pAb was used on Western blots to analyze total Erk1 and Erk2 present in various stimulated cell extracts.  Researchers also used the MEK Inhibitor U0126 demonstrate a direct inhibition of MEK.  Phospho-Erks from MEK Inhibitor U0126 studies were examined on Western blots. (0274)

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Biochem. J. 341, 363-369. p44/42 mitogen-activated protein kinase is involved in the expression of ornithine decarboxylase in leukaemia L1210 cells. 1999

Flamigni, F., Facchini, A., Capanni, C., Stefanelli, C., Tantini, B., Caldarera, C.M.

Notes: The U0126 MEK Inhibitor was used to inhibit the induction of the ornithine decarboxylase (ODC) in L1210 cells. Quiescent cells were treated with the inhibitor 30min prior to addition of complete media which induces ODC activity via a MAPK-dependent pathway. The cells were harvested after 8hr and the levels of ODC determined. The U0126 MEK Inhibitor demonstrated dose dependent inhibition of ODC and ~90% inhibition was seen with a 50-fold lower concentration than PD98059. (1159)

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J. Biol. Chem. 274, 31108-31113. Regulation of Bad phosphorylation and association with Bcl-XL by the MAPK/Erk kinase. 1999

Scheid, M.P., Schubert, K.M., Duronio, V.

Notes: The MEK Inhibitor U0126 was used to look at the role of MAPK in Bad phosphorylation. Overall phosphoBad was not overly decreased in the presence of the inhibitor but further investigation found almost complete inhibition of phosphorylation on Ser112 of Bad. (0449)

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Eur. J. Biochem. 264, 110-119. Separate roles for H-Ras and Rac in signaling by transforming growth factor (TGF)-beta: H-Ras is essential for activation of MAP kinase, partially required for transcriptional activation by TGF-beta, but not required for signaling of growth suppression by TGF-beta. 1999

Yamamoto, H., Atsuchi, N., Tanaka, H., Ogawa, W., Abe, M., Takeshita, A., Ueno, H.

Notes: Promega's MEK Inhibitor U0126 was used to block TGF-β1 dependent MAPK activation in bovine aortic endothelial cells. The inhibitor was given 15 minutes prior to a 5 minute TGF-β1 stimulation and then the cells were harvested for Western blotting. The MEK inhibitor demonstrated a dose dependent inhibition. (0132)

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J. Biol. Chem. 274, 30644-30650. Syk and Bruton's tyrosine kinase are required for B cell antigen receptor-mediated activation of the kinase Akt. 1999

Craxton, A., Jiang, A., Kurosaki, T., Clark, E.A.

Notes: The MEK Inhibitor U0126 was used to demonstrate that Erk2 phosphorylation was not required for IgM-dependent Akt phosphorylation in DT40 chicken cells. (1286)

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J. Biol. Chem. 274, 35381-35387. The MEK pathway is required for stimulation of p21WAF1/CIP1 by transforming growth factor-β. 1999

Hu, P.P., Shen, X., Huang, D., Liu, Y., Counter, C., Wang, X.-F.

Notes: The MEK Inhibitor U0126 was tested for its ability to block the TGFβ stimulation of p21 and p15 in HaCaT human keratinocytes. Experiments were performed to demonstrate that the blockage was due to MEK inhibition and not nonspecific effects on the TGFβ receptor. TGFβ can inhibit the growth of the HaCaT cells and causes a distinct morphology change. Various concentrations of U0126 were included in the culture media and found to reduce the growth inhibition to ~35% at the 50µM level from the ~70% level without the inhibitor present. The cells were treated with the TGFβ and U0126 for 18 hours. (1022)

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J. Immunol. 160, 4175-4181. Inhibition of mitogen-activated protein kinase blocks T-cell proliferation but does not induce or prevent anergy. 1998

DeSilva, D.R., Jones, E.A., Favata, M.F., Jaffee, B.D., Magolda, R.L., Trzaskos, J.M. and Scherle, P.A.

Notes: Promega's MEK Inhibitor U0126 was used in this study. (1981)

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