Recombinant zea mays Casein Kinase 2 / CK2, alpha subunit, 10 µg

Background: 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.

Recombinant zea mays casein kinase 2 alpha (Z.m. CK2 alpha), recombinantly expressed in E. coli, purified using several chromatographic steps as non fusion protein.

Protein: Casein kinase II subunit alpha, zea mays
Theoretical MW (CK2): 39.2 kDa
Expression system: E.coli
Protein concentration: 0,7 mg/ml
Purity: > 99 %
Specific activity: 1,000,000 Units*/ mg
Storage buffer: 20 mM Tris-HCl, 500 mM NaCl, 1 mM DTT, 50% glycerol, pH 8.5
Storage: - 80°C (avoid repeated freeze-thaw cycles !)
(* 1 U = 1 pmol/min at 30 degree C) using the substrate peptide RRRDDDSDDD.)

Entrez Gene ID: 542637 
UniProtKB:  P28523

Ordering information: shipped on dry ice

Product specific literature references:

Niefind K, Guerra B, Pinna LA, Issinger OG, Schomburg D (1998) "Crystal structure of the catalytic subunit of protein kinase CK2 from Zea mays at 2.1 A resolution" EMBO J. 17(9):2451-62

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

Riera M, Peracchia G, Pages M (2001) "Distinctive features of plant protein kinase CK2" Mol. Cell. Biochem. 227(1-2):119-27

Riera M, Pages M, Issinger OG, Guerra B (2003) "Purification and characterization of recombinant protein kinase CK2 from Zea mays expressed in Escherichia coli" Protein Expr. Purif. 29(1):24-32

Riera M, Figueras M, Lopez C, Goday A, Pages M (2004) "Protein kinase CK2 modulates developmental functions of the abscisic acid responsive protein Rab17 from maize" Proc. Natl. Acad. Sci. U S A. 101(26):9879-84