Caesin Kinase-2 Assay / Inhibitor Screening Kit

The CycLex® CK2 Assay / Inhibitor Screening Kit is designed to measure the activity of purified Casein Kinase-2 (CK2) for the rapid and sensitive evaluation of CK2 inhibitors or activators. The phospho-specific monoclonal antibody used in this CK2 assay kit specifically recognises the phospho-serine46 residue in p53, which is phosphorylated by CK2 in vitro.

Protein kinase CK2 is a ubiquitous and pleiotropic serine/threonine protein kinase that interacts with many different signalling pathways, especially those involved in specific phases of the cell cycle. The holoenzyme is composed of two catalytic (α and/or α’) and two regulatory (β) subunits. Both the free α/α’ catalytic subunits and the holoenzyme are constitutively active, a feature that is suspected to underlie CK2’s oncogenic potential. The enzyme is highly expressed in most cancers, and research suggests that CK2 dysregulation in tumours may influence their apoptotic activity. Thus, CK2 is an attractive target for anti-neoplastic and anti-tumour drugs.

Fig. 1 Dose dependency of the recombinant CK2 enzyme reaction, measured using the CycLex® CK2 assay kit with positive controls CK2 α/β and CK2 α’/β.

Product Information
CycLex® Casein kinase-2 (CK2) Assay / Inhibitor Screening Kit (96 wells)

Related Products

CK2 (α/β) Positive Control (4 units)

Caltag Medsystems is the distributor of MBLI’s products in the UK and Ireland. If you have any questions about these products, please contact us.

To view MBLI’s catalogue of Kinase Assay Kits, please click here.

References

Lozeman et al (1990) Isolation and characterization of human cDNA clones encoding the alpha and the alpha’ subunits of casein kinase II. Biochemistry 29 (36):8436-47

Münstermann et al (1990) Casein kinase II is elevated in solid human tumours and rapidly proliferating non-neoplastic tissue. European Journal of Biochemistry 189 (2): 251-257

Pepperkok et al (1994). Casein Kinase I1 Is Required for Transition of GdG1, Early GI, and G1/S Phases of the Cell Cycle. Journal Of Biological Chemistry 269 (9): 6986-6991

Channavajhala P, Seldin D (2002). Functional interaction of protein kinase CK2 and c-Myc in lymphomagenesis. Oncogene 21: 5280 – 5288

Desagher et al (2001). Phosphorylation of Bid by Casein Kinases I and II Regulates Its Cleavage by Caspase 8. Molecular Cell 8 (3): 602-611

Wang et al (2001). Response of cancer cells to molecular interruption of the CK2 signal Molecular and Cellular Biochemistry 227 (1-2): 167-174

Li et al (2002) Phosphorylation by Protein Kinase CK2: A Signaling Switch for the Caspase-Inhibiting Protein ARC. Molecular Cell 10 (2): 247-258