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Recombinant human Casein Kinase 2 / CK2 holo enzyme complex (alpha2, beta), 10 µg  

Recombinant human Casein Kinase 2 / CK2 holo enzyme complex (alpha2, beta), 10 µg

Recombinant human casein kinase 2 (CK2), active holo enzyme (heterotetramer ) consisting of subunits alpha2 and beta

Alternate names: casein kinase 2,CSNK2A2, CK2A2, casein kinase II subunit alpha2, CK II alpha2, 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.

Purified recombinant human CK2, subunits alpha 2 and beta expressed separately. The CK2 alpha 2 subunit was expressed with an N-terminal His-tag in E.coli. The beta subunit was expressed and purified as non-fusion protein in E.coli. Reconstitution to the alpha/beta2 holoenzyme was achieved in the course of the purification. The protein is constitutively active and thus suitable for labeling CK2 substrates. Several lines of evidence suggest a trimeric holoenzyme structure consisting of one alpha 2 and two beta molecules, in contrast to the tetrameric holoenzyme structure of a CK2 holoenzyme containing the alpha 1 subunit. .

Protein: CK2 (a2)b2 holoenzyme, active
Theoretical MW (CK2 holo): 95 kDa (fusion protein)
Expression system: E.coli
Storage buffer: 25 mM Tris-HCl, 150 mM NaCl, 1 mM DTT, pH 8.5
Storage temperature: - 80°C (avoid repeated freeze-thaw cycles !)
Protein concentration: 0.3 mg/ml (Bradford method using BSA as standard protein)
Specific activity: 2,100, 000 U*/mg
* 1 Unit is defined as 1 picomole phosphate transferred to synthetic peptide (RRRADDSDDDDD) per min at 37 °C

Entrez Gene ID:    1459/1460
UniProtKB: P19784/P67870

Ordering information: shipped on dry ice

Product specific literature references:

Grankowski N, Boldyreff B, Issinger OG (1991) "Isolation and characterization of recombinant human casein kinase II subunits alpha and beta from bacteria" Eur. J. Biochem. 198(1):25-30

Issinger OG, Brockel C, Boldyreff B, Pelton JT (1992) "Characterization of the alpha and beta subunits of casein kinase 2 by far-UV CD spectroscopy" Biochemistry 31(26):6098-103

Olsen BB, Boldyreff B, Niefind K, Issinger OG. (2006) “Purification and characterization of the CK2alpha\'-based holoenzyme, an isozyme of CK2alpha: a comparative analysis.” Protein Expr Purif.;47(2):651-61.

Olsen BB, Rasmussen T, Niefind K, Issinger OG.(2008) “Biochemical characterization of CK2alpha and alpha\' paralogues and their derived holoenzymes: evidence for the existence of a heterotrimeric CK2alpha\'-holoenzyme forming trimeric complexes.” Mol Cell Biochem. 316(1-2):37-47.

Sarno S, Ghisellini P, Pinna LA (2002) "Unique activation mechanism of protein kinase CK2. The N-terminal segment is essential for constitutive activity of the catalytic subunit but not of the holoenzyme" J. Biol. Chem. 277(25):22509-14

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