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Citations Search

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Endocrinology 148, 4371-84. Aldose reductase-regulated tumor necrosis factor-α production is essential for high glucose-induced vascular smooth muscle cell growth 2007

Ramana, K.V., Tammali, R., Reddy, A.B.M., Bhatnagar, A. and Srivastava, S.K.

Notes: Inflammation may be a key contributor to the cardiovascular diseases including heart attack and stroke that are associated with diabetes, and markers associated with inflammation, such as TNFα, that are associated with elevated cytokines are elevated in both Type 1 and Type 2 diabetes. The authors of this study looked at the response of rat vascular smooth muscle cells (VSMCs) to high glucose, and found that serum-starved VSMCs exposed to high glucose secrete TNFα. They used the SignaTECT® PKC Assay to show that the expression of the TNFa gene in response to high glucose was preceded by an increase in PKC activity. (4140)

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FASEB J. April 7, 2006, ePub ahead of print. Cyclin D1 degradation enhances endothelial cell survival upon oxidative stress. 2006

Fasanaro, P., Magenta, A., Zaccagnini, G., Cicchillitti, L., Fucile, S., Eusebi, F., Biglioli, P., Capogrossi, M.C. and Martelli, F.

Notes: Human umbilical vein endothelial cells (HUVEC) were resuspended in CaMK extraction buffer and lysed by Dounce homogenization. CaMK activity was measured using the SignaTECT® Calcium/Calmodulin-Dependent Protein Kinase (CaMK II) Assay. (3402)

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Am. J. Physiol. Renal Physiol. 290, F279-F288. Differential modulation of a polymorphism in the COOH terminus of the α-subunit of the human epithelial sodium channel by protein kinase Cδ. 2006

Yan, W., Suaud, L., Kleyman, R.K., and Rubenstein, R.C.

Notes: The authors investigated the effect of an A663T polymorphism in the alpha subunit of the human epithelial sodium channel (hENaC) on membrane trafficking. The effect of PKC-mediated phosphorylation on the intracellular trafficking of proteins containing the αT663 or the αA663 polymorphism was investigated. GST and GST-αT663 or GST-αA663 fusion proteins were subjected to in vitro phosphorylation in the presence of the SignaTECT® Assay System buffers. As a positive control for phosphorylation, the SignaTECT® Assay was performed on biotinylated neurogranin(28-43) provided in the SignaTECT® System. (3592)

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J. Biol. Chem. April 28, ePub ahead of print. Mitogenic responses of vascular smooth muscle cells to lipid peroxidation-derived aldehyde 4-hydroxy-trans-2-nonenal (HNE): Role of aldose reductase-catalyzed reduction of the HNE-glutathione conjugates in regulating cell growth. 2006

Ramana, K.V., Bhatnagar, A., Srivastava, S., Umesh C.S. Yadav, Awasthi, S., Awasthi, Y.C. and Srivastava, S.K.

Notes: Protein Kinase C activity in rat vascular smooth muscle cells in response aldose reductase was measured using the SignaTECT® Protein Kinase C (PKC) Assay System. Expression of NFκB and AP-1 was investigated by electrophoretic mobility gel shift assays using the AP-1 and NFκB Consensus Oligonucleotides. (3406)

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J. Biol. Chem. 280, 28412-28423. Protein Kinase C βII plays an essential role in dendritic cell differentiation and autoregulates its own expression. 2006

Cejas, P.J., Carlson, L.M., Zhang, J., Padmanabhan, S., Kolonias, D., Lindner, I., Haley, S., Boise, L.H. and Lee, K.P.

Notes: Protein Kinase C activity was assayed in unstimulated KG1, KG1a, KG1a-neo and KG1a-PKC-βII-GFP human leukemic cells using the SignaTECT® Protein Kinase C (PKC) Assay System. For PKC-βII promoter analysis, reporter constructs were cloned into the pGL3-Basic Vector. The pRL-CMV plasmid was used as an internal control to normalize luciferase activity. Reporter assays were carried out using the Dual-Luciferase® Reporter Assay System. (3407)

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J. Biol. Chem. 280, 20503-20508. Neurochondrin negatively regulates CaMKII phosphorylation, and nervous system-specific gene disruption results in epileptic seizure. 2005

Dateki, M., Horii, T., Kasuya, Y., Mochizuki, R., Nagao, Y., Ishida, J., Sugiyama, F., Tanimoto, K., Yagami, K., Imai, H. and Fukamizu, A.

Notes: SignaTECT® Calcium/Calmodulin-Dependent Protein Kinase (CaMKII) Assay System was used to determine CaMKII activity in mouse hippocampus lysates. (3401)

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J. Biol. Chem. 278(36), 33730-33737. Ca2+-calmodulin-dependent protein kinase II potentiates store-operated Ca2+ current. 2003

Machaca, K.

Notes: This study investigated the effect of CaMKII on store-operated calcium entry (SOCE).  To do this, Xenopus laevis oocytes were depleted of intracellular calcium stores by treating with thapsigargin for 3 hours.  The oocytes were then injected with an RNA encoding  constitutively active CaMKII.  After homogenization in 80mM β-glycerophosphate, 20mM HEPES pH 7.5, 15mM MgCl2, 1mM DTT, 1mM sodium vanadate, 50mM NaF plus protease inhibitor cocktail, CaMKII activity was assayed using the SignaTECT Calcium/Calmodulin-Dependent Protein Kinase (CaM KII) Assay System. (2750)

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Arterioscler. Thromb. Vasc. Biol. 22, 901-906. Divergence of angiogenic and vascular permeability signaling by VEGF inhibition of protein kinase C suppresses VEGF-induced angiogenesis, but promotes VEGF-induced, NO-dependent vascular permeability.  2002

Spyridopoulos, I., Luedemann, C., Chen, D., Kearney, M., Chen, D., Murohara, T., Principe, N., Isner, J.M. and Losordo, D.W.

Notes: The Myristoylated Protein Kinase C Peptide Inhibitor and cAMP-Dependent Protein Kinase Peptide Inhibitor were used in cell and animal studies to help specifically identify Protein Kinase A and C activities. The researchers used a range of 0-12uM Myristoylated Protein Kinase C Peptide Inhibitor for the studies. Protein Kinase A and C activities were measured using the SignaTECT® cAMP-Dependent Protein Kinase (PKA) Assay and SignaTECT® Protein Kinase C (PKC) Assay Systems, respectively. Experiments were performed in human umbilical vein endothelial cells (HUVECs), bovine aortic endothelial cells, mouse corneas, and guinea pigs.  (3130)

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Eur. J. Neurosci. 16, 777-786. Lack of PSD-95 drives hippocampal neuronal cell death through activation of an alpha CaMKII transduction pathway. 2002

Gardoni, F., Bellone, C., Viviani, B., Marinovich, M., Meli, E., Pellegrini-Giampietro, D.E., Cattabeni, F. and Di Luca, M.

Notes: The SignaTECT® Calcium/Calmodulin-Dependent Protein Kinase (CaM KII) Assay System was used to analyze CaMKII activity in hippocampal and cortical primary cell cultures incubated with and without the CaM KII inhibitor KN-93. The results were expressed as percent activity compared to a control reaction. (2638)

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J. Biol. Chem. 275, 13571-13579. Calcineurin promotes protein kinase C and c-Jun NH2-terminal kinase activation in the heart: Cross-talk between cardiac hypertrophic signaling pathways 2000

De Windt, L.J., Lim, H.W., Haq, S., Force, T., Molkentin, J.D.

Notes: The SignaTECT® Protein Kinase C Assay System was used to measure PKC activity in mouse left ventricles. The tissue was homogenized then run over a DEAE column prior to assay. Excellent detail is provided for the tissue preparation. (1262)

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EMBO J. 19(12), 2946-2957. Phosphorylation status of the SCR homeodomain determines its functional activity: Essential role for protein phosphatase 2A,B'. 2000

Berry, M. and Gehring, W.

Notes: The Serine-Threonine Phosphatase Assay System was used to monitor dephosphorylation of two phosphopeptides derived from the SCR homeodomain. Dephosphorylation was performed using the catalytic subunit of the PP2A protein. Authors also used pSI for cloning, protein kinase A enzyme, PKA and PKC assays using biotinylated peptides (SignaTECT® Protein Kinase assay systems), anti-β-galactosidase for Drosophila embryo staining, and TNT® Quick Coupled Transcription/Translation systems to produce mutant and wild type protein for gel shifts. (2150)

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J. Biol. Chem. 275, 13377-13385. Stimulation of protein kinase C modulates insulin-like growth factor-1-induced Akt activation in PC12 cells. 2000

Zheng, W.-H. , Kar, S. , Quirion, R.

Notes: The pretreatment of PC12 cells with 20µM U0126 MEK Inhibitor for 20min prior to phorbol ester and IGF-1 treatment blocked the phosphorylation of Akt kinase. To determine the effect of PKC inhibitors on PKC activity in the PC12 cells after phorbol ester stimulation, lysates were prepared from various cellular fractions and analyzed for PKC activity with the SignaTECT® PKC Assay System. Control values were obtained in the absence of the lipid activator solution and in the presence of the Myristoylated PKC Inhibitor Peptide. The greatest increase in PKC activity was found in the membrane fraction. (0058)

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Mol. Pharmacol. 55, 118-125. Daunorubicin- and mitoxantrone-triggered phosphatidylcholine hydrolysis: Implication in drug-induced ceramide generation and apoptosis. 1999

Bettaieb, A., Plo, I., Mansat-de Mas, V., Quillet-Mary, A., Levade, T., Laurent, G. and Jaffrezou, J.-P.

Notes: The SignaTECT® Protein Kinase C Assay System was used to measure PKC activity in extracts of U937 human monocytic leukemia cells in the presence or absence of different drugs. Good detail on the preparation of cell extracts is provided. (1442)

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Am. J. Physiol. 276, H786-H792. Proapoptotic effects of ANG II in human coronary artery endothelial cells: Role of AT1 receptor and PKC activation. 1999

Li, D., Yang, B., Philips, M.I., Mehta, J.L.

Notes: The SignaTECT® Protein Kinase C Assay System was used to determine PKC activity in extracts of human coronary artery endothelial cells. The cells were induced into apoptosis by treatment with angiotensin II which was inhibitable with PKC inhibitors. (0791)

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Am. J. Physiol. 275, H568-H576. Ox-LDL induces apoptosis in human coronary artery endothelial cells: role of PKC, PTK, bcl-2, and Fas. 1998

Li, D., Yang, B., Mehta, J.L.

Notes: The authors used the SignaTECT® Protein Kinase Assay System (PKC) and SignaTECT® Protein Tyrosine Kinase Assay System (PTK) to study kinase activity in human coronary artery endothelial cells. The Myristoylated PKC peptide inhibitor was used to study repression of PKC activity. (0792)

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J. Biol. Chem. 272, 20063-20069. Adrenocorticotropin Induction of Stress-activated Protein Kinase in the Adrenal Cortex in vivo 1997

Watanabe, G., Pena, P., Albanese, C., Wilsbacher, L.D., Young, J.B. and Pestell, R.G.

Notes: The SignaTECT® Protein Kinase C (PKC) Assay System was used in this study. (2191)

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J. Clin. Invest. 100, 1180-1192. Stimulus coupling to transcription versus secretion in pheochromocytoma cells: Convergent and divergent signal transduction pathways and the crucial roles for route of cytosolic calcium entry and protein kinase C. 1997

Tang, K., Wu, Mahata, S.K., Mahata, M., Gill, B.M., Parmer, R.J. and O’Conner, D.T.

Notes: Kinase assays were performed on PC12 cell extracts. A lot of detail is given on preparation of cell extracts. Kinase activities were measured in the cytosol and membrane fractions. Kinase activities were determined in the presence or absence of 1mM nicotine. The SignaTECT® Protein Kinase C (PKC) and cAMP-Dependent (PKA) Protein Kinase Assay Systems were used in this study. (1532)

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