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Recombinant human Casein kinase 2 holo enzyme complex (alpha2 C336S, beta2), 10 µg  

Recombinant human Casein kinase 2 holo enzyme complex (alpha2 C336S, beta2), 10 µg

Recombinant human Casein kinase 2 (CK2), active holo enzyme (heterotetramer) consisting of subunits alpha2 C336S, beta2

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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PK-CK2ABHM2-A010

Availability: within 3 days

255,00 €

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 human recombinant CK2 hole enzyme, subunits alpha 2 C336S and beta expressed separately, CK2 (alpha 2) with a N-terminal His-tag in E. coli, beta as non-fusion protein in E. coli. Reconstituted to the holoenzyme in the course of the purification. Constitutively active. Suitable for labeling CK2 substrates. Purified by several chromatography steps (Ni-sepharose,heparin, gel-filtration). CK2 (alpha 2) C336S does not form intermolecular disulfide bridges via the C-terminal Cysteine 336. Size exclusion analysis suggests a tetrameric holoenzyme structure with two CK2 (alpha 2) and two CK2 beta subunits.

Protein: CK2 (a2)2 C336S; beta2 holoenzyme, active
Theoretical MW (CK2 holo): 135 450 Da (fusion protein)
Expression system: E.coli
Storage buffer: 50 mM Tris-HCl, 500 mM NaCl, 10 mM DTT, pH 8.5
Storage temperature: - 80°C (avoid repeated freeze-thaw cycles !)
Protein concentration: 0.5 mg/ml (Bradford method using BSA as standard protein)
Specific activity: 1,740, 029 U*/mg
* 1 Unit is defined as 1 picomole phosphate transferred to synthetic peptide (RRRADDSDDDDD) per min at 30 °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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