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Recombinant human Casein kinase 2 / CK2 alpha2 (C336S mutant) subunit, 10 µg  


Recombinant human protein kinase Casein Kinase 2 / CK2, alpha subunit 2 (hCK2 alpha2), CK2 (alpha 2) subunit, C336S mutant, catalytic subunit

Alternate names: CSNK2A1, CK2A2, CKIIalpha, casein kinase II subunit alpha2, CK2 alpha 2

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Availability: on stock

255,00 €

Background: Protein kinase CK2 (Casein kinase II) C336S mutant, 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 (alpha 2) C336S expressed in E. coli with a N-terminal His-tag. Constitutively active. Suitable for labelling CK2 substrates. Purified by several chromatography steps (Ni-Sepharose, Heparin). The CK2 (alpha 2) subunit is a paralog of CK2 (alpha 1), mainly differing in the C-terminal sequence. CK2 (alpha 2) C336S does not form intermolecular disulfide bridges via the C-terminal Cysteine 336. The crystal structure of N-terminal His-tagged CK2 (alpha 2) C336S has been described.

Protein: CK2 alpha 2
Theoretical MW (CK2 alpha2): 42.8 kDa
Expression system: E.coli
Protein concentration: 0.5 mg/ml
Purity: > 95 %
Specific activity: 841,819 Units*/ mg
Storage buffer:50 mM Tris-HCl, 500 mM NaCl, 10 mM DTT, pH 8.5.
Storage: - 80°C (avoid repeated freeze-thaw cycles !)
(* 1 Unit is defined as 1 picomole phosphate transferred to synthetic peptide (RRRDDDSDDD per min at 37° C)

Entrez Gene: 1459

UniProtKB: P19784

Ordering information: shipped on dry ice

Product specific literature references:

Bischoff N, Olsen B, Raaf J, Bretner M, Issinger OG, Niefind K. (2011) “Structure of the human protein kinase CK2 catalytic subunit CK2α' and interaction thermodynamics with the regulatory subunit CK2β.” J Mol Biol. 18;407(1):1-12.

Lozeman FJ, Litchfield DW, Piening C, Takio K, Walsh KA, Krebs EG (1990) "Isolation and characterization of human cDNA clones encoding the alpha and the alpha\' subunits of casein kinase II" Biochemistry 29(36):8436-47

Munstermann U, Fritz G, Issinger OG et al. (1990) "Casein kinase II is elevated in solid human tumours and rapidly proliferating non-neoplastic tissue" Eur J Biochem. 189(2):251-7

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

Yamaguchi Y, Wada T, Suzuki F, Takagi T, Hasegawa J, Handa H (1998) "Casein kinase II interacts with the bZIP domains of several transcription factors" Nucleic Acids Res. 26(16):3854-61

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

McKendrick L, Milne D, Meek D (1999) "Protein kinase CK2-dependent regulation of p53 function: evidence that the phosphorylation status of the serine 386 (CK2) site of p53 is constitutive and stable" Mol Cell Biochem. 191(1-2):187-99

Bosc DG, Luscher B, Litchfield DW (1999) "Expression and regulation of protein kinase CK2 during the cell cycle" Mol Cell Biochem. 191(1-2):213-22

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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