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J. Immunol. 184, 4801-9. Regulatory B cells (B10 cells) have a suppressive role in murine lupus: CD19 and B10 cell deficiency exacerbates systemic autoimmunity 2010

Watanabe, R., Ishiura, N., Nakashima, H., Kuwano, Y., Hitoshi, O., Tamaki, K., Shinichi, S., Tedder, T.F. and Fujimoto, M.

Notes: B cells purified from single-cell mouse splenocyte suspensions were resuspended in medium and then stimulated with goat anti-mouse IgM Ab F(ab´)2 fragments and then lysed. Lysates were either incubated with phosphospecific antibodies (Anti-ACTIVE® MAPK or JNK Ab) or analyzed for tyrosine kinase activity using the ProFluor™ Src-Family Kinase Assay. (4139)

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J. Biol. Chem. 281, 4663-4670. Apoptotic cells, at all stages of the death process, trigger characteristic signaling events that are divergent from and dominant over those triggered by necrotic cells. 2006

Patel, V., Longacre, A., Hsiao, K., Fan, H., Meng, F., Mitchell, J.E., Rauch, J., Ucker, D.S. and Levine, J.S.

Notes: Serum-starved, bone marrow-derived macrophages were exposed to apoptotic or necrotic cells, or latex beads (control), and phosphorylation of a variety of signaling molecules was investigated by Western blot. Anti-ACTIVE® MAPK pAb, Anti-ACTIVE® p38 pAb, Anti-ACTIVE® JNK pAb and Anti-ERK 1/2 pAb were used. (3428)

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Clin. Can. Res. 11, 8295-8303. Ghrelin and a novel pregroghrelin isoform are highly expressed in prostate cancer and ghrelin activates mitogen-activated protein kinase in prostate cancer. 2005

Yeh, A.H., Jeffery, P.L., Duncan, R.P., Herington, A.C. and Chopin, L.K.

Notes: Serum-starved PC3 and LNCaP prostate cancer cells were treated with various concentrations of ghrelin over a time course. Western blots of cell lysates were probed with Anti-ACTIVE® JNK pAb, Anti-ACTIVE® p38 pAb, Anti-ACTIVE® MAPK pAb and Anti-ERK(1/2) pAb to assess activation of MAPK pathways. (3434)

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Blood 105, 4685-4692. Src homology 2 domain-containing inositol-5-phosphatase 1 (SHIP1) negatively regulates TLR4-mediated LPS response primarily through a phosphatase activity- and PI-3K-independent mechanism. 2005

An, H., Xu, H., Zhang, M., Zhou, J., Feng, T., Qian, C., Qi, R. and Cao, X.

Notes: The authors of this study investigated the role of Src homology 2 (SH2) domain-containing inositol-5-phosphatase 1 (SHIP1) in Toll-like receptor 4 (TLR4)-mediated lipopolysaccharide (LPS) response. RAW264.7 macrophages were transfected with wildtype or mutant SHIP1 or control plasmid. Anti-ACTIVE® JNK and p38 antibodies were used in Western analyses to determine phosphorylation of these kinases in response to overexpression of SHIP1 or mutant SHIP1. To investigate any effects on IκB-alpha and NF-κB expression, RAW264.7 macrophages were cotransfected with pGL3-XκB-luciferase reporter plasmid and pRL-TK Renilla luciferase control plasmid. Transfected cells were treated with LPS for 6 hours or left untreated (control). The Dual-Luciferase® Reporter Assay System was used to monitor reporter gene expression. (3524)

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Cell Death Differ. 10, 153-162. Down regulation of caspases and Fas ligand expression, and increased lifespan of neutrophils after transmigration across intestinal epithelium 2003

Le'Negrate, G., Rotagno, R., Auberger, P., Rossi, B., Hofman, P.

Notes: Anti-ACTIVE® JNK pAb was used in immunoblot analysis of  human polymorphonuclear leukocyte protein lysates. (2665)

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J. Biol. Chem. 278, 3860-3867. Enhanced activation of mitogen-activated protein kinase and myosin light chain kinase by the Pro33 polymorphism of integrin beta 3. 2003

Vijayan K.V., Liu Y., Dong J.F. and Bray P.F.

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.  (2789)

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Neurochem. Int. 38, 341-347. Differential regulation of JNK activation and MKP-1 expression by peroxovanadium complexes. 2001

Rumora, L., Shaver, A., Zanic-Grubisic, T., and Maysinger, D.

Notes: The effect of bisperoxovanadium complexes, known protein tyrosine phosphatase inhibitors, on the activation of JNK was examined in a number of cell lines, including HeLa, PC12 and OVCAR-3. The level of dually phosphorylated (activated) JNK was determined by Western blot analysis using a 1:1000 dilution of Promega's Anti-ACTIVE® JNK pAb. (2381)

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J. Neurochem. 76, 1010-21. Dopaminergic cell death induced by MPP(+), oxidant and specific neurotoxicants shares the common molecular mechanism 2001

Chun, H.S., Gibson, G.E., DeGiorgio, L.A., Zhang, H., Kidd, V.J., and Son J.H.

Notes: A number of neurotoxins linked with Parkinson's Disease induce apoptosis and activate the JNK signaling pathway in the nigral dopaminergic cell line SN4741. Activation of JNK was also monitored in dopaminergic neurons in mouse brain by immunofluorescent double labeling for tyrosine hydroxylase and active (dually phosphorylated) JNK protein. Brain sections were permeabilized with 0.2% Triton® X-100 and stained with a 1:100 dilution of the Anti-ACTIVE® JNK pAb. (2453)

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J. Biol. Chem. 276, 13113-13120. Mechanisms underlying neuronal death induced by chromogranin A-activated microglia. 2001

Ciesielski-Treska, J., Ulrich, G., Chasserot-Golaz, S., Zwiller, J., Revel, M.O., Aunis, D., and Bader M.F.

Notes: The neurotoxic effects of chromogranin A activated microglia in neurodegenerative diseases was examined. Rat neurons were grown in the presence or absence of conditioned media from chromogranin A treated or untreated microglia. DNA fragmentation in apoptotic neurons was detected using the DeadEnd™ Fluorometric TUNEL System. The levels of dually phosphorylated, active JNK in these cells was determined by Western blot analysis using the Anti-ACTIVE® JNK pAb. A pan JNK antibody was used to normalize for total JNK protein on the Western blots. (2378)

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J. Biol. Chem. 276, 16374-16378. N-terminal domains of the class IA phosphoinositide 3-kinase regulatory subunit play a role in cytoskeletal but not mitogenic signaling. 2001

Hill, K.M., Huang, Y., Yip, S.C., Yu, J., Segall, J.E., and Backer, J.M.

Notes: The mechanism of lamellipod extension in the metastatic breast cancer cell line MTLn3 cells was studied to determine the signaling pathways involved. The cells were microinjected with a protein-protein interaction domain which inhibits lamellipod extension and incubated in the absence or presence of 1 M sorbitol for 30 minutes. Cells were then fixed in 10% paraformaldehyde, permeabilized with methanol, blocked with 1% bovine serum albumin/5% donkey serum, and immunostained with the Anti-ACTIVE® JNK antibodies to measure JNK activation. (2383)

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J. Neurosci. 20, 4506-14. Activation of mitogen-activated protein kinases after transient forebrain ischemia in gerbil hippocampus. 2000

Sugino, T., Nozaki. K., Takagi, Y., Hattori, I., Hashimoto, N., Moriguchi, T., and Nishida, E.

Notes: The role of JNK, p38 and MAPK signaling pathways in delayed neuronal death after transient forebrain ischemia was examined using Western blotting and immunohistochemistry. Gerbil hippocampi were homogenized, subjected to SDS-PAGE, blotted to PVDF membranes and incubated with one of the following primary antibodies: Anti-ACTIVE® JNK pAb (1:2000 dilution), Anti-ACTIVE® p38 pAb (1:1000 dilution), and the Anti-ACTIVE® MAPK pAb (1:2000 dilution).The secondary antibody was the Donkey Anti-Rabbit IgG (H+L), AP, diluted 1:10,000 for JNK and p38 and 1:5000 for ERK. For immunohistochemistry, gerbils were perfused with 4% paraformaldehyde. Frozen 40µm sections were stained with either the Anti-ACTIVE® JNK pAb and the Anti-ACTIVE® p38 pAb. (2402)

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Neurosci. Lett. 278, 101-104. Activation of mitogen-activated protein kinases in gerbil hippocampus with ischemic tolerance induced by 3-nitroproprionic acid. 2000

Sugino, T., Nozaki, K., Hashimoto, N.

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. (0313)

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J. Cell Biol. 150, 165-175. Glutamate slows axonal transport of neurofilaments in transfected neurons. 2000

Ackerley, S., Grierson, A.J., Brownlees, J., Thornhill, P., Anderton, B.H., Leigh, P.N., Shaw, C.E., and Miller C.C.

Notes: The authors seek to determine the role of glutamate in excitotoxicity and neurofilament accumulation seen in some neurodegenerative diseases. Neurofilament light, middle, and heavy chains were expressed from rat cDNAs cloned into the pCI-neo Mammalian Expression vector in SW-13 cells. Primary rat cortical neurons were transfected with a neurofilament middle chain and green fluorescent fusion protein. SW13 cells and primary rat cortical neurons were transfected with the ProFection® Mammalian Transfection System–Calcium Phosphate. The CytoTox 96® Non-Radioactive Cytotoxicity Assay was used to monitor glutamate toxicity in these cell. To determine the role of the MAPK and JNK signaling pathways,  SW13- cells and primary neuronal cells were immunostained for dually phosphorylated MAPK and JNK using Promega's Anti-ACTIVE® MAPK pAb and Anti-ACTIVE® JNK pAb, respectively. Cells were fixed in 4% paraformaldehyde, permeabilized in 0.1% Triton® X-100 in PBS, blocked with  0.2% Tween® 20 in TBS, and incubated with primary antibodies diluted in blocking solution. Western blot analyses were performed on the primary cortical neurons to quantitate the level of dually phosphorylated MAPK protein  The blots were also probed with a pan MAPK antibody that detects total (active and inactive) MAPK. (2382)

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Mol. Cell. Biol. 20, 6826-6836. Hsp72-mediated suppression of c-Jun N-terminal kinase is implicated in development of tolerance to caspase-independent cell death. 2000

Gabai, V.L., Yaglom, J.A., Volloch, V., Meriin, A.B., Force, T., Koutroumanis, M., Massie, B., Mosser, D.D. and Sherman, M.Y.

Notes: Levels of active (phophorylated) JNK were tested by western blotting of extracts from heat shocked fibroblasts using the Anti-ACTIVE® JNK pAb. Severe heat shock strongly activates JNK, but this activation is suppressed when cells are first exposed to a mild heat shock. It was shown that when accumulation of Hsp72 protein after mild heat stress was blocked by expression of antisense RNA, JNK suppression was relieved. The fibroblasts used were IMR90 human lung fibroblasts. (2131)

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J. Biol. Chem. 275(28), 21247-21254. MAPK Upstream Kinase (MUK)-binding Inhibitory Protein, a Negative Regulator of MUK/Dual Leucine Zipper-bearing Kinase/Leucine Zipper Protein Kinase 2000

Fukuyama, K. , Yoshida, M. , Yamashita, A. , Deyama, T. , Baba, M. , Suzuki, A. , Mohri, H. , Ikezawa, Z. , Nakajima, H. , Hirai, S. , and Ohno, S.

Notes: The 293T cell line was transfected with constructs expressing MAPK Upstream Kinase (MUK) or another JNK activating Kinase called COT. Together with the MUK or COT, cells were transfected with JNK constructs and MUK Inhibitory Binding Protein. The coexpression of MUK or COT with JNK caused activation of JNK to its dually phosphorylated form. Inclusion of MIBP with MUK decreased the activation of JNK to near basal levels. MIBP had no effect on COT-dependent JNK activation. Activation of JNK was determined with the Anti-ACTIVE® JNK pAb via Western blotting. (0072)

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J. Cell Biol. 149(3), 741-754. Matrix Survival Signaling: From Fibronectin via Focal Adhesion Kinase to c-Jun NH2-terminal Kinase 2000

Almeida, E.A.C. , Ili, D. , Han, Q. , Hauck, C.R., Jin, F., Kawakatsu, H. , Schlaepfer, D.D. , and Damsky, C.H.

Notes: The authors used the Anti-Active JNK pAb. The paper uses primary rabbit synovial fibroblasts grown on fibronectin or a collagen matrix which leads to JNK activation. (0071)

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Neurosci. Lett. 294, 117-120. Phosphorylation of c-Jun NH(2)-terminal kinase and p38 mitogen-activated protein kinase after transient forebrain ischemia in mice. 2000

Takagi, Y., Nozaki, K., Sugino, T., Hattori, I., and Hashimoto, N.

Notes: The role of JNK and p38 mitogen-activated protein kinase during transient brain ischemia was examined by immunohistochemistry and Western blot analysis. The authors findings indicate that JNK and p38 MAPK pathways may play important roles in neuronal death during brain ischemia. Levels of active JNK and p38 in mouse brain were determined by Western blot analysis and immunohistochemistry using the Anti-ACTIVE® JNK pAb and the Anti-ACTIVE® p38 pAb. For Western blot analysis the antibodies were diluted 1:5000 while immunohistochemical studies were done with dilutions of 1:1000 and 1:400, respectively. Both JNK and p38 were activated following reperfusion of the ischemic tissue. (2409)

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J. Biol. Chem. 275, 11114-11120. Regulatory mechanisms of TRAF2-mediated signal transduction by Bcl10, a MALT lymphoma-associated protein. 2000

Yoneda, T., Imaizumi, K., Maeda, M., Yui, D., Manabe, T., Katayama, T., Sato, N., Gomi, F., Morihara, T., Mori, Y., Miyoshi, K., Hitomi, J., Ugawa, S., Yamada, S., Okabe, M., and Tohyama, M.

Notes: The signaling mechanism of Bcl10, an apoptosis-associated gene mutated in mucosa-associated lymphoid tissue lymphomas, was examined. Activation of the JNK signaling pathway in response to overexpression of Bcl10 in 293 cells was monitored by immunoprecipitation with an anti-JNK1 antibody followed by Western blotting with the Anti-ACTIVE® JNKpAb. Immunohistochemical staining of transgenic mice expressing Bcl10 was also performed with the Anti-ACTIVE® JNK pAb. Mouse thymus was fixed in 4% paraformaldehyde, dehydrated, embedded in paraffin, and sectioned (5 µm thick) prior to immunostaining. (2384)

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Mol. Biol. Cell 11, 3751-3763. Sequential activation of ERK and repression of JNK by scatter factor/hepatocyte growth factor in madin-darby canine kidney epithelial cells. 2000

Paumelle, R., Tulasne, D., Leroy, C., Coll, J., Vandenbunder, B., and Fafeur, V.

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. (2379)

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EMBO J. 19, 4955-4966. SRF-dependent gene expression is required for PI3-kinase-regulated cell proliferation 2000

Poser, S., Impey, S., Trinh, K., Xia, Z. and Storm D.R.

Notes: The Anti-ACTIVE® JNK pAb was used to detect JNK in lysates of agonist- and inhibitor-treated PC12 cells. The antibody was used at a 1:5000 dilution, and the secondary antibodies used were either HRP- or AP-conjugated. The authors were studying the PI3K pathway, and used various inhibitors to differentiate the regulatory pathway controlled by PI3K from other kinase pathways. The cells were treated with NGF to stimulate kinase activity, and treated with kinase inhibitors to determine which inhibitors were selectively inhibited PI3K signaling. (2135)

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Mol. Cell. Biol. 20(9), 3015-3026. TAK1 participates in c-Jun n-terminal kinase signaling during Drosophila development. 2000

Takatsu, Y., Nakamura, M., Stapleton, M., Danos, M.C., Matsumoto, K., O'Connor, M.B., Shibuya, H., Ueno, N.

Notes: The authors used the Anti-ACTIVE® JNK pAb to probe western blots of Drosophila larval extracts for in vivo phosphorylation caused by ectopic expression of TAK1. (2212)

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Mol. Cell. Biol. 20(14), 5184-5195. The docking protein HEF1 is an apoptotic mediator at focal adhesion sites 2000

Law, S.F., O'Neill, G.M., Fashena, S.J., Einarson, M.B. and Golemis, E.A.

Notes: The authors used the Anti-ACTIVE® JNK pAb to probe activation of the JNK pathway by HEF1 and colocalization of active JNK and HEF1 at focal adhesion sites in MCF-7 cells that inducibly overexpress the HEF1 protein. Western blots were performed to observe activation of JNK (antibody dilution 1:5,000), and detected by chemiluminescence. ICC was detected with a rhodamine-labeled secondary goat anti-rabbit from Molecular Probes. Fixed and permeablized cells were incubated with primary antibody for 1 hour. (2145)

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J. Biol. Chem. 275, 18810-18817. The inhibition of interleukin-6-dependent STAT activation by mitogen-activated protein kinases depends on tyrosine 759 in the cytoplasmic tail of glycoprotein 130. 2000

Terstegen, L., Gatsios, P., Bode, J.G., Schaper, F., Heinrich, P.C., and Graeve, L.

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. (2380)

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Nat. Cell Biol. 2, 346-51. Tollip, a new component of the IL-1RI pathway, links IRAK to the IL-1 receptor. 2000

Burns, K., Clatworthy, J., Martin, L., Martinon, F., Plumpton, C., Maschera, B., Lewis, A., Ray, K., Tschopp, J., and Volpe, F.

Notes: Activation of JNK in response to interleukin-1 treatment of 293 cells transfected with a type I IL-1 receptor expression plasmid was quantitated. Extracts of 293T cells were subjected to Western blot analysis with the Anti-ACTIVE® JNK pAb (1:5000 dilution) to detect the active, dually phosphorylated forms of JNK. (2459)

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J. Biol. Chem. 274, 6272-6279. An inhibitor of p38 mitogen-activated protein kinase protects neonatal cardiac myocytes from ischemia. 1999

Mackay, K., Mochly Rosen, D.

Notes: Authors use the Anti-ACTIVE® JNK pAb for western blot analysis in their studies on ventricular myocytes from day old Sprague-Dawley rats. (0719)

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