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| 1. |
Hsu, C.Y., Bristow, R., Cha, M.S., Wang, B.G., Ho, C.L., Kurman, R.J., Wang, T.L., Shih, Ie.M.
(2004)
Characterization of active mitogen-activated protein kinase in ovarian serous carcinomas.
Clin. Cancer Res.
10
,
6432-6436
.
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Notes:
The Anti-ACTIVE® MAPK polyclonal antibody was used to immunohistochemically stain and type patient ovarian serous carcinomas. The researchers used a 1:500 dilution of the antibody on paraffin fixed tissue sections on tissue microarrays. A secondary peroxidase staining kit was used to complete the immunohistochemical staining. In these studies, the ovarian serous carcinomas displayed increased MAPK expression and activity. Western blots were also performed on tissue lysates using a 1:3000 dilution of the antibody.
(0003210) |
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Products: Anti-ACTIVE® MAPK pAb, Rabbit, (pTEpY) |
| 2. |
Barnabé-Heider F. and Miller F.D.
(2003)
Endogenously produced neurotrophins regulate survival and differentiation of cortical progenitors via distinct signaling pathways.
J. Neurosci.
23
,
5149 – 5160
.
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Notes:
This paper describes a study of the effect of endogenous neurotrophins on cortical neuron development. Cortical progenitor cells were isolated from mouse embryos and cultured. These precursor cells express both BDNF and NT-3 as well as the corresponding TrkB and TrkC receptors. BDNF and NT-3 signal via Trk receptors to activate the PI3-kinase and MEK pathways. These pathways serve distinct functions, PI3-kinase being essential for progenitor survival and MEK for the differentiation of neurons but not glial cells. The progenitor cell cultures were treated with either Anti-Human BDNF pAb or Anti-Human NT-3 pAb at 20μg/ml to block the function of the endogenous neurotrophins. Anti-ACTIVE® MAPK pAb was used to assess levels of activated MAPK by Western blotting of cell extracts.
(0002778) |
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Products: Anti-ACTIVE® MAPK pAb, Rabbit, (pTEpY) | Anti-Human BDNF pAb | Anti-Human NT-3 pAb |
| 3. |
Vijayan K.V., Liu Y., Dong J.F. and Bray P.F.
(2003)
Enhanced activation of mitogen-activated protein kinase and myosin light chain kinase by the Pro33 polymorphism of integrin beta 3.
J. Biol. Chem.
278
,
3860-3867
.
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Notes:
The role of integrin alpha(IIb)beta(3) in focal adhesion kinase activation and MAPK signaling was studied using Chinese hamster ovary and human kidney 293 cell lines expressing either the Leu(33) or Pro(33) isoform of beta(3). Compared with Leu(33) cells, Pro(33) cells demonstrated substantially greater activation of ERK2 (but not MAPK family members JNK and p38) upon adhesion to immobilized fibrinogen (but not fibronectin), and upon integrin cross-linking. ERK2 activation was mediated through MAPK kinase and required phosphoinositide 3-kinase signaling and an intact actin cytoskeleton. Levels of activated MAPK family members ERK1 and 2, JNK, and p38 were assessed by western blotting using Anti-ACTIVE® MAPK (1:5000 dilution), Anti-ACTIVE® JNK (1:5000 dilution), and Anti-ACTIVE® p38 (1:1000 dilution) pAbs. Anti-ERK 1/2 pAb was used at a 1:5000 dilution as a control for total protein amounts loaded on the blots.
(0002789) |
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Products: Anti-ACTIVE® JNK pAb, Rabbit, (pTPpY) | Anti-ACTIVE® MAPK pAb, Rabbit, (pTEpY) | Anti-ACTIVE® p38 pAb, Rabbit, (pTGpY) | Anti-ERK 1/2 pAb, Rabbit |
| 4. |
Ochi, H., Ogino, H., Kageyama, Y. and Yasuda, K.
(2003)
The stability of the lens-specific Maf protein is regulated by Fibroblast Growth Factor (FGF)/ERK signaling in lens fiber differentiation.
J. Biol. Chem.
278
,
537-544
.
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Notes:
Fibroblast growth factor (FGF) signaling is necessary for proliferation and differentiation of chicken lens cells. The transcription factor L-Maf is a lens differentiation factor that appears to mediate FGF signaling. This paper shows that L-Maf is repressed by FGF/ERK signaling and that L-Maf is phosphorylated by ERK. Both Anti-ACTIVE MAPK® pAb and Anti-ERK1/2 pAb were used to determine MAPK levels by Western blotting. Anti-ACTIVE® MAPK pAb was also used in immunocytochemistry analysis of cultured chick lens cells.
(0002773) |
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Products: Anti-ACTIVE® MAPK pAb, Rabbit, (pTEpY) | Anti-ERK 1/2 pAb, Rabbit |
| 5. |
Henrich, L.M., Smith, J.A., Kitt, D., Errington, T.M., Nguyen, B., Traish, A.M. and Lannigan, D.A.
(2003)
Extracellular signal-regulated kinase 7, a regulator of hormone-dependent estrogen receptor destruction.
Mol. Cell. Biol.
23
,
5979-5988
.
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Notes:
This paper investigates the mechanism of estrogen receptor alpha (ERalpha) degradation. Loss of ER is associated with aggressive breast tumors and poor clinical outcome. ERK7 is shown to be a specific regulator of ERalpha degradation in human breast cells. Several members of the MAPK family were examined to determine if they regulate ERK7 turnover. Levels of activated MAPK were examined by Western blotting of extracts of BHK cells that had been co-transfected with different kinases. The Anti-ACTIVE® MAPK pAb was used to detect dually phosphorylated ERK p42/p44 in these lysates. Overexpression of ERK7 was shown to specifically enhance degradation of ERalpha in BHK cells. ERK7 and active MAPK levels were assessed in breast cancer cell lines as well as normal and cancerous human breast tissue. Lowered ERK7 levels correlated with ERalpha-positive tumors, suggesting that loss of ERK7 leads to higher levels of ERalpha in these cancers.
(0002769) |
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Products: Anti-ACTIVE® MAPK pAb, Rabbit, (pTEpY) |
| 6. |
Cottom J., Salvador, L.M., Maizels, E.T., Reierstad, S., Park, Y., Carr, D.W., Davare, M.A., Hell, J.W., Palmer, S.S., Dent, P., Kawakatsu, H., Ogata, M. and Hunzicker-Dunn, M.
(2003)
Follicle-stimulating hormone activates extracellular signal-regulated kinase but not extracellular signal-regulated kinase kinase through a 100-kDa phosphotyrosine phosphatase.
J. Biol. Chem.
278
,
7167-7179
.
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Notes:
This paper investigates the pathway by which follicle stimulating hormone (FSH) activates ERKs (MAPK) p42 and p44 in rat primary granulosa cells. The phosphorylation state of MAPK p42/p44 was assessed by Western blotting using the Anti-ACTIVE® MAPK pAb. Phosphorylated MAPKs were localized to the nucleus of granulosa cells by immunocytochemistry using Anti-ACTIVE® MAPK pAb. Cells were stimulated, fixed with 3.7% formaldehyde, permeabilized with 1% Triton X-100 in PBS, washed, blocked for 1 hour in 1% bovine serum albumin in PBS and incubated overnight at 4°C with a 1:100 dilution of the antibody in PBS containing 1% bovine serum albumin.
(0002768) |
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Products: Anti-ACTIVE® MAPK pAb, Rabbit, (pTEpY) |
| 7. |
Cao, W., Sohn, U.D., Bitar, K.N., Behar, J., Biancani, P. and Harnett, K.M.
(2003)
MAPK mediates PKC-dependent contraction of cat esophageal and lower esophageal sphincter circular smooth muscle.
Am. J. Physiol. Gastrointest. Liver Physiol.
285
,
G86–G95
.
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Notes:
Esophageal contraction has been shown to be protein kinase C (PKC) dependent. These authors examined the involvement of ERK1/ERK2 and p38 MAPKs in PKC-dependent esophageal (ESO) circular muscle contraction and lower esophageal sphincter (LES) contraction. Feline ESO and LES circular smooth muscle was homogenized and the level of phosphorylated MAPK was studied by Western blotting using the Anti-ACTIVE MAPK® pAb.
(0002771) |
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Products: Anti-ACTIVE® MAPK pAb, Rabbit, (pTEpY) |
| 8. |
Piwien-Pilipuk, G., MacDougald, O. and Schwartz, J.
(2002)
Dual regulation of phosphorylation and dephosphorylation of C/EBPbeta modulate its transcriptional activation and DNA binding in response to growth hormone.
J. Biol. Chem.
277
,
44557-44565
.
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Notes:
The transcription factor CCAAT/enhancer-binding protein beta (C/EBPbeta) occurs in cells as the transcriptional activator liver-enriched activating protein (LAP) and, in truncated form, as liver-enriched inhibitory protein (LIP), which inhibits transcription. Previous studies have shown that growth hormone (GH) promotes dephosphorylation of both LAP and LIP. This study investigated phosphorylation states of LAP and LIP by isoelectric focusing (IEF). IEF revealed that GH not only promotes dephosphorylation, but also promotes rapid and transient phosphorylation of murine C/EBPbeta on Thr188 in mLAP and Thr37 in mLIP, sites that correspond to the conserved mitogen-activated protein kinase (MAPK) consensus sequence. Western blotting of 3T3-F442A cell lysates showed a correlation between activation of MAPK (ERK1/2) and phosphorylation of C/EBPbeta. Active MAPK was measured using the Anti-ACTIVE MAPK® pAb, and total ERK levels were measured by Western blotting with Anti-ERK1/2 pAb.
(0002774) |
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Products: Anti-ACTIVE® MAPK pAb, Rabbit, (pTEpY) | Anti-ERK 1/2 pAb, Rabbit |
| 9. |
Abe, K, and Saito, H.
(2001)
Possible linkage between glutamate transporter and mitogen-activated protein kinase cascade in cultured rat cortical astrocytes.
J. Neurochem.
76
,
217-23
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Notes:
A possible linkage between glutamate signalling and the MAPK cascade in rat primary cortical astrocytes was examined. Levels of activated, dually phosphorylated MAPK were determined using the Anti-ACTIVE® MAPK pAb whereas total MAPK levels were monitored with the Anti-ERK 1/2 pAb, Rabbit. The MEK inhibitor U0126 at 1µm completely abolished ERK phosphorylation in response to glutamate release. Following SDS-PAGE, total protein was transferred to a PVDF membrane and blotted with a 1:5000 dilution of the Anti-ERK 1/2 pAb, Rabbit or a 1:10000 dilution of the Anti-ACTIVE® MAPK pAb overnight at 4°C.
(0002390) |
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Products: Anti-ACTIVE® MAPK pAb, Rabbit, (pTEpY) | Anti-ERK 1/2 pAb, Rabbit |
| 10. |
Ishii, T., Satoh, E. and Nishimura, M.
(2001)
Integrin-linked kinase controls neurite outgrowth in N1E-115 neuroblastoma cells.
J. Biol. Chem.
276
,
42994-43003
.
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Notes:
The function of Integrin Linked Kinase (ILK) in cell interactions with extracellular matrix was studied. ILK activation is an important event in the integrin-mediated signal pathway and is necessary for neurite outgrowth in serum-starved mouse N1E-115 neuronal cells on laminin. Activation of p38 MAP kinase is necessary for the ILK-mediated signal leading to integrin-dependent neurite outgrowth. Activation of MEK and ERK does not appear to be involved in this process. Both Anti-ACTIVE® MAPK pAb and Anti-ERK1/2 pAb were used to assess levels of active and total p42/p44 in cell extracts by Western blotting.
(0002770) |
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Products: Anti-ACTIVE® MAPK pAb, Rabbit, (pTEpY) | Anti-ERK 1/2 pAb, Rabbit |
| 11. |
Zavadil, J., Bitzer, M., Liang, D., Yang, Y.C., Massimi, A., Kneitz, S., Piek, E., and Bottinger, E.P.
(2001)
Genetic programs of epithelial cell plasticity directed by transforming growth factor-beta.
Proc. Natl. Acad. Sci. U S A
98
,
6686-91
.
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Notes:
The transcriptional targets of the MAPK pathway in a TGFβ1 induced model of epithelial-mesenchymal transitions are explored. Activation of MAPK signaling regulated genes with functions in cell-matrix adhesion and endocytosis. Human keratinocytes were cultured in the absence or presence of 15µM U0126. To monitor MAPK activation and inhibition, the Anti-ACTIVE® MAPK pAb was used in Western blots to detect the dually phosphorylated form of MAPK. Results were normalized to total level of active and inactive MAPK by Western blot analysis with the Anti-ERK 1/2 pAb, Rabbit.
(0002389) |
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Products: Anti-ACTIVE® MAPK pAb, Rabbit, (pTEpY) | Anti-ERK 1/2 pAb, Rabbit |
| 12. |
Lee, J., Klessig, D.F., and Nurnberger, T.
(2001)
A harpin binding site in tobacco plasma membranes mediates activation of the pathogenesis-related gene HIN1 independent of extracellular calcium but dependent on mitogen-activated protein kinase activity.
Plant Cell
13
,
1079-93
.
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Notes:
Harpin proteins are a group of effector proteins involved in plant pathogenesis of several phytopathogenic bacteria. The role of these proteins in pathogenesis was examined and the authors found that MAPK activation is required. Activated MAPK was detected by Western blot analysis with an antibody raised specifically against the dually phosphorylated (active) form of MAPK. Thirty micrograms of tobacco protein extract was separated by SDS-PAGE, transferred to nitrocellulose membrane, and blotted with the Anti-ACTIVE® MAPK pAb. A secondary goat anti-rabbit IgG antibody coupled to alkaline phosphatase was used to visualize the immunoreactive proteins.
(0002397) |
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Products: Anti-ACTIVE® MAPK pAb, Rabbit, (pTEpY) |
| 13. |
Le, F., Stomski, F., Woodcock, J.M., Lopez, A.F., Gonda, T.J.
(2000)
The role of disulfide-linked dimerization in interleukin-3 receptor signaling and biological activity.
J. Biol. Chem.
275
,
5124-5130
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Notes:
The CellTiter 96® Non-Radioactive Cell Proliferation Assay (MTT) was used to determine the effects of the expression of wildtype IL-3 receptor α and wildtype or mutant β. The proliferation of the transfected CTL-EN (an IL-2-dependent CTLL-2 cell derivative) was measured after 72 hours in the presence of IL-3. Both mutants and wildtype receptors activated Erk 1 & 2 as judged by Western blotting of cell extracts with the Anti-ACTIVE® MAPK pAb.
(0000849) |
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Products: Anti-ACTIVE® MAPK pAb, Rabbit, (pTEpY) | CellTiter 96® Non-Radioactive Cell Proliferation Assay |
| 14. |
Jovanovic, J.N., Czernik, A.J., Fienberg, A.A., Greengard, P., and Sihra, T.S.
(2000)
Synapsins as mediators of BDNF-enhanced neurotransmitter release.
Nat. Neurosci.
3
,
323-29
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Notes:
Treatment of brain-derived neurotrophic factor increased MAPK-dependent synapsin I phosphorylation in rat cerebral cortex synaptosomal preparations. MAPK activity was determined by Western blot analysis using the Anti-ACTIVE® MAPK (1:10,000 dilution) pAb to detect the dually phosphorylated forms of MAPK. CaM kinase II activity was assayed by Western blot analysis with the Anti-ACTIVE® CaM KII pAb, Rabbit, (pT286) (1:2500 dilution). The Anti-Mouse IgG (H+L), AP Conjugate (1:1000 dilution) was used as a secondary antibody in Western blot analysis to detect TrkB expression.
(0002393) |
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Products: Anti-ACTIVE® CaM KII pAb, Rabbit, (pT286) | Anti-ACTIVE® MAPK pAb, Rabbit, (pTEpY) | Anti-Mouse IgG (H+L), AP Conjugate |
| 15. |
Terstegen, L., Gatsios, P., Bode, J.G., Schaper, F., Heinrich, P.C., and Graeve, L.
(2000)
The inhibition of interleukin-6-dependent STAT activation by mitogen-activated protein kinases depends on tyrosine 759 in the cytoplasmic tail of glycoprotein 130.
J. Biol. Chem.
275
,
18810-18817
.
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Notes:
The effect of suppressor of cytokine signaling (SOCS) expression on the Jak/STAT, MAPK, JNK, and p38 signaling pathways was examined in HepG2, Cos-7, and NIH 3T3 cells. Both PMA and bFGF (Promega) resulted in a rapid upregulation of SOCS-3 expression. MAPK, JNK, and p38 activation was monitored by Western blot analysis using the Anti-ACTIVE® MAPK Anti-ACTIVE® JNK pAb, and the Anti-ACTIVE® p38 pAb. Total levels of active and inactive MAPK protein was determined using the Anti-ERK 1/2 pAb, Rabbit.
(0002380) |
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Products: Anti-ACTIVE® JNK pAb, Rabbit, (pTPpY) | Anti-ACTIVE® MAPK pAb, Rabbit, (pTEpY) | Anti-ACTIVE® p38 pAb, Rabbit, (pTGpY) |
| 16. |
Sakamoto, H., Kitamura, T., and Yoshimura, A.
(2000)
Mitogen-activated protein kinase plays an essential role in the erythropoietin-dependent proliferation of CTLL-2 cells.
J. Biol. Chem.
275
,
35857-62
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Notes:
The mechanism of erythropoietin receptor signaling via MAP kinase activation was examined. Mouse IL2-dependent cytotoxic T cell lines were stimulated with 10 units/ml erythropoietin, MAPK was immunoprecipitated, subjected to SDS-PAGE, and transferred onto PVDF membranes. The dually phosphorylated forms of MAPK were detected by Western blot using the Anti-ACTIVE® MAPK pAb antibody.
(0002396) |
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Products: Anti-ACTIVE® MAPK pAb, Rabbit, (pTEpY) |
| 17. |
Harada, Y., Sanada, K., and Fukada, Y.
(2000)
Circadian activation of bullfrog retinal mitogen-activated protein kinase associates with oscillator function.
J. Biol. Chem.
275
,
37078-85
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Notes:
The vertebrate retina retains a circadian oscillator that seems to correspond to an in vivo circadian rhythm in MAPK phosphorylation. Activation of MAPK in bullfrog retinas was monitored by Western blot analysis using the Anti-ACTIVE® MAPK pAb (1:1000 dilution). Proteins were separated by SDS-PAGE, transferred to PVDF membranes and incubated at 4°C overnight with the Anti-ACTIVE® MAPK pAb.
(0002400) |
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Products: Anti-ACTIVE® MAPK pAb, Rabbit, (pTEpY) |
| 18. |
Sugino, T., Nozaki, K., Hashimoto, N.
(2000)
Activation of mitogen-activated protein kinases in gerbil hippocampus with ischemic tolerance induced by 3-nitroproprionic acid.
Neurosci. Lett.
278
,
101-104
.
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Notes:
Gerbils were treated with 3-nitropropionic acid intraperitoneally for 1 to 4 days. Sections of the CA1 area of the hippocampus were analyzed for activation of various mitogen activated kinases. The c-Jun N-terminal kinase was activated by the treatment as judged by immunohistochemistry of 40µm frozen sections with the Anti-ACTIVE® JNK pAb.
(0000313) |
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Products: Anti-ACTIVE® JNK pAb, Rabbit, (pTPpY) | Anti-ACTIVE® MAPK pAb, Rabbit, (pTEpY) |
| 19. |
Paumelle, R., Tulasne, D., Leroy, C., Coll, J., Vandenbunder, B., and Fafeur, V.
(2000)
Sequential activation of ERK and repression of JNK by scatter factor/hepatocyte growth factor in madin-darby canine kidney epithelial cells.
Mol. Biol. Cell
11
,
3751-3763
.
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Notes:
The authors characterize the cell signaling pathways triggered by the multifunctional growth factor scatter factor/hepatocyte growth factor. In Madin-Darby Canine Kidney epithelial cells SF/HGF induces phosphorylation of MAPK while stimulating weakly and then repressing phosphorylation of JNK. The Anti-ACTIVE® MAPK pAb and Anti-ACTIVE® JNKpAb were used to quantitate the level of activation of the MAPK and JNK signaling pathways by Western blot analysis.
(0002379) |
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Products: Anti-ACTIVE® JNK pAb, Rabbit, (pTPpY) | Anti-ACTIVE® MAPK pAb, Rabbit, (pTEpY) |
| 20. |
Lee, B.N., and Elion, E.A.
(1999)
The MAPKKK Ste11 regulates vegetative growth through a kinase cascade of shared signaling components.
Proc. Natl. Acad. Sci. U S A
96
,
12679-84
.
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Notes:
The involvement of mitogen-activated protein kinase kinase kinase kinase (Ste20), MAPKKK (Ste11), MAPKK (Ste7), and transcription factor (Ste12) under the basal conditions of vegetative growth of yeast was examined. Saccharomyces cerevisiae protein was subjected to Western blot analysis with the Anti-ACTIVE® MAPK Ab (1:1500 dilution) to monitor levels of active MAPK.
(0002399) |
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Products: Anti-ACTIVE® MAPK pAb, Rabbit, (pTEpY) |
| 21. |
O'Prey, J., Leslie, N., Itoh, K., Ostertag, W., Bartholomew, C., Harrison, P.R.
(1998)
Both stroma and stem cell factor maintain long-term growth of ELM erythroleukemia cells, but only stroma prevents erythroid differentiation in response to erythropoietin and interleukin-3
Blood
91
,
1548-1555
.
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Notes:
The CellTiter 96® Non-Radioactive Cell Proliferation Assay was used to assess the growth factor requirements of murine erythroleukemia cells in culture. The cells were cultured for five days with various cytokines and growth factors prior to assay. Several of the IGF-1 independent clones analyzed by western blotting with the Anti-ACTIVE® MAPK pAb were found to have a constitutive level of activated MAP Kinase. Study also shows serum is a very potent activator of MAPK in serum-starved cells.
(0000567) |
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Products: Anti-ACTIVE® MAPK pAb, Rabbit, (pTEpY) | CellTiter 96® Non-Radioactive Cell Proliferation Assay |
| 22. |
Rui, H., Xu, J., Mehta, S., Fang, H., Williams, J., Dong, F., and Grimley, P.M.
(1998)
Activation of the Jak2-Stat5 signaling pathway in Nb2 lymphoma cells by an anti-apoptotic agent, aurintricarboxylic acid.
J. Biol. Chem.
273(1)
,
28-32.
.
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Notes:
The MTT-based CellTiter 96® Non-Radioactive Cell Proliferation Assay was used to measure the viability of serum-deprived prolactin-dependent Rat lymphoma Nb2 cells cultured in the presence of ovine prolactin and aurintricarboxylic acid (ATA). ATA was demonstrated to stimulate growth of Nb2 cells and protect against staurosporine-induced apoptosis. Promega’s Anti-ACTIVE™ MAPK pAb was used on Western blots to demonstrate that ATA stimulates phosphorylation of MAPK.
(0001702) |
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Products: Anti-ACTIVE® MAPK pAb, Rabbit, (pTEpY) | CellTiter 96® Non-Radioactive Cell Proliferation Assay |
| 23. |
Crow, T., Xue-Bian, J.J., Siddiqi, V., Kang, Y., and Neary J.T.
(1998)
Phosphorylation of mitogen-activated protein kinase by one-trial and multi-trial classical conditioning.
J. Neurosci.
18
,
3480-87
.
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Notes:
In sea slugs (Hermissenda crassicornis) the protein kinase C pathway is involved in short- and long-term memory associated with multi-trial Pavlovian conditioning. The authors examine the activation of MAPK pathway by one-trial and multi-trial conditioning in Hermissenda eyes and proximal optic nerves. The dually phosphorylated, active MAPK was detected by Western blot using the Anti-ACTIVE® MAPK pAb.
(0002398) |
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Products: Anti-ACTIVE® MAPK pAb, Rabbit, (pTEpY) |
| 24. |
Abe, M.K., Kartha, S., Karpova, A.Y., Li, J., Liu, P.T., Kuo, W.-L. and Hershenson, M.B.
(1998)
Hydrogen peroxide activates extracellular signal-regulated kinase via protein kinase C, Raf-1 and MEK1.
Am. J. Respir. Cell Mol. Biol.
18
,
562-569.
.
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Notes:
Bovine tracheal myocytes were treated with hydrogen peroxide and the level of MAPK phosphorylation was determined by Western blotting of the cell lysates with the Anti-ACTIVE® MAPK pAb. Pretreatment of the cells with the hydroxyly radical scavenger MPG significantly reduced the level of activation. Pretreatment of the cells with heavy metal chelator o-phenanthroline had very little effect.
(0002051) |
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Products: Anti-ACTIVE® MAPK pAb, Rabbit, (pTEpY) |
| 25. |
Gorenne, I. , Su, X. , Moreland, R. S.
(1998)
Inhibition of p42 and p44 MAP kinase does not alter smooth muscle contraction in swine carotid artery.
Am. J. Physiol.
275
,
H131-H138
.
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Notes:
Authors use the Anti-ACTIVE® MAPK pAb in Western blots and kinase studies on swine carotid arteries.
(0001112) |
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Products: Anti-ACTIVE® MAPK pAb, Rabbit, (pTEpY) |