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Mol. Cell. Biol. 24, 6205-6214. Rac1 Inhibits Apoptosis in Human Lymphoma Cells by Stimulating Bad Phosphorylation on Ser-75. 2004

Zhang, B., Zhang, Y., and Shacter, E.

Notes: Researchers used Promega’s cAMP-Dependent Protein Kinase Peptide Inhibitor to demonstrate that BAD kinase is phosphorylated through a cAMP-Dependent Protein Kinase (PKA) dependent pathway in Burkitt’s lymphoma BL-41 cells.  The PepTag® Non-Radioactive cAMP-Dependent Protein Kinase Assay was used to demonstrate PKA activity in BL-41 cell lysates.  In these experiments the researchers added cAMP with and without Promega’s cAMP-Dependent Protein Kinase Peptide Inhibitor (20μM) or Rp-cAMPS (100μM) to 0.2-2ug of BL-41 cell lysate.  Images of gels were depicted in the paper. (3134)

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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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J. Biol. Chem. 275, 14360-14366. Protein kinase A associates with cystic fibrosis transmembrane conductance regulator via an interaction with Ezrin 2000

Sun, F., Hug, M.J., Bradbury, N.A., Frizzell, R.A.

Notes: Immunoprecipitates of CFTR become phosphorylated upon addition of a PKA catalytic subunit which is inhibitable by the Protein Kinase A Inhibitor Peptide. The SignaTECT® cAMP-Dependent Protein Kinase Assay System was used to measure PKA activity in immunoprecipitates of the CFTR protein. The activity was almost totally inhibited by the Protein Kinase A Inhibitor Peptide. PKA activity was four times higher with the anti-CFTR antibody precipitates than with a control antibody and addition of cAMP increased the amount of phosphorylation observed in the immunoprecipitates. Immunoprecipitates were prepared from Calu-3 human airway epithelia cells. (0318)

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J. Biol. Chem. 274, 10625-10632. Identification of enhanced serine kinase activity in insulin resistance. 1999

Qiao, L., Goldberg, J.L., Russell, J.C., Sun, X.J.

Notes: The phosphorylation of rat Insulin Receptor 1 was investigated with cell lysates. The cAMP-Dependent Protein Kinase Peptide Inhibitor and Myristoylated Protein Kinase C Peptide Inhibitor were included in separate reactions to define which kinase was performing the phosphorylation. (0525)

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J. Biol. Chem. 272, 14617-14623. Transforming growth factor-beta1 inhibits type I inositol 1,4,5- trisphosphate receptor expression and enhances its phosphorylation in mesangial cells. 1997

Sharma, K., Wang, L., Zhu, Y., Bokkala, S., Joseph, S.K.

Notes: This reference details use of the c-AMP-Dependent Protein Kinase Peptide Inhibitor. (0429)

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