CycLex® Casein Kinase2 (CK2) Assay/Inhibitor Screening kit from MBL International

CycLex® Casein Kinase2 (CK2) Assay/Inhibitor Screening kit from MBL International
Product CycLex® Casein Kinase2 (CK2) Assay/Inhibitor Screening kit
Company MBL International
Price
More Information View Company Product Page
Detection Request Info
Target CK2 (Casein kinase II)
Catalog Number CY-1170
Method Assay/Inhibitor Screen
Original Item Name CycLex® Casein Kinase2 (CK2) Assay/Inhibitor Screening kit
Quantity 96 wells
Target/Molecule Descriptor CycLex®

Description

Protein kinase CK2 is a ubiquitous and pleiotropic serine/threonine protein kinase, which appears to interact with different signaling pathways and therefore represents the prototype of a multifunctional protein kinase. The holoenzyme is generally composed of two catalytic (alpha and/or alpha) and two regulatory (beta) subunits (1-3). Although the beta subunits deeply affect many properties of CK2, both the free alpha/alpha catalytic subunits and the holoenzyme are constitutively active. The enzyme is highly expressed in most cancers (4) and this higher expression has been tentatively correlated with the involvement of CK2 in the promotion of specific phases of the cell cycle (5). Unlike the majority of protein kinases, which are tightly regulated enzymes, CK2 is endowed with high constitutive activity, a feature that is suspected to underlie its oncogenic potential (6, 7) and possible implication in viral infections. This makes CK2 an attractive target for anti-neoplastic and antiviral drugs. Experimental studies suggest that dysregulated expression of the alpha subunit of CK2 imparts an oncogenic potential in the cells such that in cooperation with certain oncogenes (8, 9), it produces a profound enhancement of the tumor phenotype. Recent studies have provided evidence that overexpression of CK2 in tumor cells is not simply a reflection of tumor cell proliferation alone but additionally may reflect the pathobiological characteristics of the tumor. Of considerable interest is the possibility that CK2 dysregulation in tumors may influence the apoptotic activity in those cells (10-12). Approaches to interfering with the CK2 signal may provide a useful means for inducing tumor cell death (13). Measurement of CK2 activity The protocol generally regarded as most sensitive for the quantitative measurement of CK2 activity involves incubation of the CK2 sample with substrate (either a natural or synthetic polypeptide such as CK2 substrate peptide; RRRDDDSDDD), in the presence of Mg2+ and 32P-labeled ATP. The reaction is terminated by "spotting" a sample onto a filter paper disc, followed by immersion in acid to precipitate the radiolabeled product. The filter papers are then washed extensively to remove unincorporated radiolabel and the radioactivity is counted. While sensitive, this method is labor-intensive, generates hazardous radioactive waste and depends on a radioisotope with a short half-life. It is particularly unsuitable when kinase assays are only performed on an infrequent basis. The CycLex® CK2 Assay/Inhibitor Screening Kit uses a peroxidase coupled anti-phospho-p53 serine46 monoclonal antibody as a reporter molecule in a 96-well ELISA format. This assay provides a non-isotopic, sensitive, and specific method to measure CK2 activity.

References

1. Lozeman, F.J., Litchfield, D.W., Piening, C., Takio, K., Walsh, K.A. and Krebs, E.G. (1990) Isolation and characterization of human cDNA clones encoding the ÃŽ± and ÃŽ±Ã‚´ subunits of CK2. Biochemistry 29, 8436aEUR"8447 2. Litchfield, D.W., Lozeman, F.J., Piening, C., Sommercorn, J., Takio, K., Walsh, K.A. and Krebs, E.G. (1990) Subunit structure of CK2 from bovine testis: demonstration that the ÃŽ± and ÃŽ±Ã‚´ subunits are distinct polypeptides. J. Biol. Chem. 265, 7638aEUR"7644 3. Maridor, G., Park, W., Krek, W. and Nigg, E.A. (1991) CK2. cDNA sequences, developmental expression and tissue distribution of mRNAs for ÃŽ±, ÃŽ±Ã‚´ and ÃŽ² subunits of the chicken enzyme. J. Biol. Chem. 266, 2362aEUR"2368 4. Munstermann, U., Fritz, G., Seitz, G., Lu, Y.P., Schneider, H.R. and Issinger, O.-G. (1990) CK2 is elevated in solid human tumors and rapidly proliferating non-neoplastic tissue. Eur. J. Biochem. 189, 251aEUR"257 5. Pepperkok, R., Lorenz, P., Ansorge, W. and Pyerin, W. (1994) CK2 is required for transition of G0/G1, early G1, and G1/S phases of the cell cycle. J. Biol. Chem. 269, 6986aEUR"6991 6. Landesman-Bollag, E., Romieu-Mourez, R., Song, D.H., Sonenshein, G.E., Cardiff, R.D. and Seldin, 0 10 20 30 40 50 60 70 80 90 100 110 0 50 100 150 200 Heparin (ng/ml) Relative intensity (% of control) CKIIÃŽ±+CKIIÃŽ² CKIIÃŽ±+CKIIÃŽ² IC50; CKIIÃŽ±+CKIIÃŽ²: 65ng/ml CKIIÃŽ±aEUR™+CKIIÃŽ²: 20 ng/ml CK2 Assay/Inhibitor Screening Kit Users Manual Cat# CY-1170 4 H Constitution Way · Woburn, MA 01801 · Phone: 1.800.200.5459 · Fax: 781-939-6963 · www.mblintl.com 14 Version #040611-1 D.C. (2001) Protein kinase CK2 in mammary gland tumorigenesis. Oncogene 20, 3247aEUR"3257 7. Seldin, D.C. and Leder, P. (1995) CK2 alpha transgene-induce murine lymphoma: relation to theileriosis in cattle. Science 267, 894aEUR"897 8. Landesman-Bollag, E., Channavajhala, P.L., Cardiff, R.D. and Seldin, D.C. (1998) p53 deficiency and mis-expression of protein kinase CK2a collaborate in the development of thymic lymphomas in mice. Oncogene 16, 2965aEUR"2974 9. Channavajhala, P. and Seldin, D.C. (2002) Functional interaction of protein kinase CK2 and c-Myc in lymphomagenesis. Oncogene 21, 5280aEUR"5288 10. Sayed, M., Pelech, S., Wong, C., Marotta, A. and Salh, B. (2001) Protein kinase CK2 is involved in G2 arrest and apoptosis following spindle damage in epithelial cells. Oncogene 20, 6994aEUR"7005 11. Desagher, S., Osen-Sand, A., Montessuit, S., Magnenat, E., Vilbois, F., Hochmann, A., Journot, L., Antonsson, B. and Martinou, J.C. (2001) Phosphorylation of bid by casein kinases I and II regulates its cleavage by caspase 8. Mol. Cell 8, 601aEUR"611 12. Li, P., Li, J., Muller, E., Otto, A., Dietz, R. and von Harsdorf, R. (2002) Phosphorylation by protein kinase CK2. A signaling switch for the caspase-inhibiting protein ARC. Mol. Cell 10, 247aEUR"258 13. Wang, H., Davis, A., Yu, S. and Ahmed, K. (2001) Response of cancer cells to molecular interruption of the CK2 signal. Mol. Cell. Biochem. 227, 167aEUR"174

Specifications/Features

For Research use only. Not for use in diagnostic procedure.

MBL International Contact Information

MBL International
4 H Constitution Way
Woburn, MA 01801

Customer Service: 800-200-5459

Fax Number: 781-939-6963

Web Site: http://mblintl.com

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