cycLex Cdi1/KAP Protein Phosphatase Fluorometric Assay Kit-Discontinued

  • Code # cy-1356
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    This product has been discontinued.

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Citations
  1. Hyeog Kang, Jeong-Yong Suh, Young-Sang Jung, Jae-Won Jung, Myung K. Kim, Jay H. Chung; Peptide Switch Is Essential for Sirt1 Deacetylase Activity. Mol. Cell. 44, 203, 2011,
  2. Shan-Shan Yu, Yi Cai1, Jian-Tao Ye, Rong-Biao Pi, Shao-Rui Chen, Pei-Qing Liu, Xiao-Yan Shen, Yong Ji; Sirtuin 6 protects cardiomyocytes from hypertrophy in vitro via inhibition of NF-κB-dependent transcriptional activity. Br J Pharmacol. 168: 117-28. 2012
References
  1. Gyuris, J.; Golemis, E.; Chertkov, H.; Brent, R. Cdi1, a human G1 and S phase protein phosphatase that associates with Cdk2. Cell, 75: 791-803, 1993.
  2. Hannon, G. J.; Casso, D.; Beach, D. KAP: a dual specificity phosphatase that interacts with cyclin-dependent kinases. Proc. Nat. Acad. Sci. 91: 1731-1735, 1994.
  3. Poon RY and Hunter T. Dephosphorylation of Cdk2 Thr160 by the cyclin-dependent kinase-interacting phosphatase KAP in the absence of cyclin. Science, 270: 90-3, 1995.
  4. Denu, J. M., M. A. Stuckey, M. Saper, and J. E. Dixon. Form and function in protein dephosphorylation. Cell, 87: 361-364, 1996.
  5. Kinzler, K. W., and B. Vogelstein. Landscaping the cancer terrain. Science, 280: 1036-1037, 1998.
  6. Parsons, R. Phosphatases and tumorigenesis. Curr. Opin. Oncol. 10: 88-91, 1998.
  7. Lee SW, Reimer CL, Fang L, Iruela-Arispe ML, Aaronson SA. Overexpression of kinase-associated phosphatase (KAP) in breast and prostate cancer and inhibition of the transformed phenotype by antisense KAP expression. Mol Cell Biol. 20: 1723-32, 2000