Protein kinase CK2 (Casein kinase II) is an ubiquitous and highly conserved protein serine/threonine kinase that is typically found in tetrameric complexes consisting of two catalytic (alpha and/or alpha') subunits and two regulatory beta subunits. CK2 has a number of physiological targets and participates in a complex series of cellular functions including the maintenance of cell viability. It has long been considered to play a role in cell growth and proliferation and considerable evidence suggests that it can also exert potent suppression of apoptosis in cells. In normal cells, the level of CK2 appears to be tightly regulated, and cells resist a change in their intrinsic level of CK2. However, in all the cancers that have been examined an elevation of CK2 has been observed. Recent evidence suggests that CK2 can exert an anti-apoptotic role by protecting regulatory proteins from caspase-mediated degradation. Furthermore, the anti-apoptotic function of CK2 may contribute to its ability to participate in transformation and tumorigenesis.
Human recombinant casein kinase 2 holo enzyme (hCK2 holo) containing alpha and beta subunits which were separately expressed in E. coli as non-fusion proteins and purified using several chromatographic steps. The holo enzyme (alpha2beta2) has been reconstituted in the course of the purification and is highly activ suitable for labeling CK2 substrates. Mw 140 kDa, purity >95% by SDS-PAGE, no protease activity detectable, specific activity > 1.200.000 U/mg (1 U = 1 pmol/min at 37 degree C) using the substrate peptide RRRDDDSDDD.
Size: 10 µg
Ordering information: shipped on dry ice
Product specific literature references:
Bidwai AP, Reed JC, Glover CV (1993) "Phosphorylation of calmodulin by the catalytic subunit of casein kinase II is inhibited by the regulatory subunit" Arch. Biochem. Biophys. 300(1):265-70
Robitzki A, Bodenbach L, Voss H, Pyerin W (1993) "Human casein kinase II. The subunit alpha protein activates transcription of the subunit beta gene" J. Biol. Chem. 268(8):5694-702
Bodenbach L, Fauss J, Robitzki A, Krehan A, Lorenz P, Lozeman FJ, Pyerin W (1994) "Recombinant human casein kinase II. A study with the complete set of subunits (alpha, alpha' and beta), site-directed autophosphorylation mutants and a bicistronically expressed holoenzyme" Eur. J. Biochem. 220(1):263-73
Chester N, Yu IJ, Marshak DR (1995) "Identification and characterization of protein kinase CKII isoforms in HeLa cells. Isoform-specific differences in rates of assembly from catalytic and regulatory subunits" J. Biol. Chem. 270(13):7501-14
Dobrowolska G, Lozeman FJ, Li D, Krebs EG (1999) "CK2, a protein kinase of the next millennium" Mol. Cell. Biochem. 191(1-2):3-12
Battistutta R, Sarno S, De Moliner E, Marin O, Issinger OG, Zanotti G, Pinna LA (2000) "The crystal structure of the complex of Zea mays alpha subunit with a fragment of human beta subunit provides the clue to the architecture of protein kinase CK2 holoenzyme" Eur. J. Biochem. 267(16):5184-90
Benitez MJ, Cochet C, Jimenez JS (2001) "A surface plasmon resonance study of the interactions between the component subunits of protein kinase CK2 and two protein substrates, casein and calmodulin" Mol. Cell. Biochem. 227(1-2):31-6
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