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Recombinant human Casein Kinase 2 / CK2, holo enzyme complex (alpha1, beta), 10 µg  

Recombinant human Casein Kinase 2 / CK2, holo enzyme complex (alpha1, beta), 10 µg

Recombinant human casein kinase 2 (CK2), active holo enzyme (heterotetramer ) consisting of alpha (1-335) and beta subunit, CK2a2b2

Alternate names: casein kinase 2 alpha 1, CK2A1, CKII alpha, CKII alpha1, CSNK2A1 /CSNK2B, CKII beta, CSK2B, CK2B, G5A, Phosphitin, casein kinase 2 beta,  CK2 holoenzyme, CK2 holo, CK2 heterotetramer, CK2a2b2

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265,00 €

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.

PLEASE NOTE: To increase stability of the holo complex hCK2 holo consist of shortened alpha subunits (aa1-335)  and beta subunits.

Human recombinant casein kinase 2 holo enzyme (hCK2 holo) containing alpha (aa1-335)  and beta subunits expressed separately in E. coli as non-fusion proteins, purified by several chromatography steps (HiTrapQ, Heparin agarose, Superdex200) and reconstituted to the CK2 alpha2beta2 holoenzyme in the course of purification. Since CK2 alpha is unstable and prone to degradation, CK2 subunits alpha was shortened at the C-terminus to obtain a stable, crystallizable alpha subunit. The holo enzyme is constitutively activ suitable for labeling CK2 substrates.

Protein: CK2 (a1)b2 holoenzyme, active
Theoretical MW (CK2 holo): 135 kDa (fusion protein)
Expression system: E.coli
Storage buffer: 25 mM Tris-HCl, 500 mM NaCl, 1 mM DTT, pH 7.5
Storage temperature: - 80°C (avoid repeated freeze-thaw cycles !)
Protein concentration: 0.5 mg/ml (Bradford method using BSA as standard protein)
Specific activity: 2,390 000 U*/mg
* 1 Unit is defined as 1 picomole phosphate transferred to synthetic peptide (RRRDDDSDDD) per min at 37° C

Entrez Gene ID: 1457/1460 
UniProtKB:  P68400/P67870

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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