Casein Kinase 2, α-subunit
human, recombinant, E. coli
For in vitro use only!
Shipping: shipped on dry ice
Storage Conditions: store at -80 °C
avoid freeze/thaw cycles
Shelf Life: 12 months
Molecular Weight: 45.1 kDa
Accession number: M55265
Purity: > 90 % (SDS-PAGE)
Form: liquid (Supplied in 25 mM Tris-HCl pH 8.5, 500 mM NaCl, 1 mM DTT, 500 μM PMSF and 50% glycerol)
Activity: > 1 U/mg (1 Unit is defined as 1 micromole phosphate transferred to synthetic peptide RRRDDDSDDD (cat.# PE-207) per min at 37 °C).
Casein kinase 2 (CK2) is a ubiquitous pleiotropic proliferation-associated serine/threonine protein kinase. The enzyme is probably present in all eukaryotic cells, implying that it has fundamental cellular functions. Similar to protein kinase A, CK2 is a tetramer containing 2 α- or α-prime subunits (or one of each) and 2 β-subunits. The β-subunit fills a regulatory role in the holoenzyme. The catalytic α-subunit corresponds to the C-subunit of PKA, the non-catalytic β-subunit is unique and differs from the R-subunit of PKA in all known features. The α-/α-prime subunits are the catalytic subunits with distinct sequences and are encoded by different genes (Boldyreff et al., 1992, Wirkner et al., 1992, Yang-Feng et al., 1991). Whereas the CK2 α-subunit is found ubiquitously in all cells and organs the CK2 α-prime subunit is preferentially found in brain and testis (Guerra et al., 1999). Recently it was shown that the β-subunit is trifunctional: (i) it confers stability to the holoenzyme, (ii) it increases enzyme activity and (iii) it determines substrate specificity. The human recombinant protein kinase CK2α1 was expressed in E. coli as a non fusion protein and purified by several chromatography steps. The α-subunit is constitutively active and suitable for labeling casein kinase 2 alpha substrates. It is shown to be extremely salt sensitive, the highest activity is shown without salt.
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