The Casein kinase 2 (EC 126.96.36.199) is a serine/threonine-selective protein kinase that is a tetramer of two alpha subunits and two beta subunits. The alpha subunits have the catalytic kinase domain. Casein kinase 2 has been implicated in cell cycle control, DNA repair, regulation of the circadian rhythm and other cellular processes.
CK II, Recombinant (Human)
Casein Kinase II (CK2) is a constitutively active serine/threonine protein kinase composed of two 44 kDa catalytic α-subunits and two 26 kDa regulatory β-subunits in an α2β2 configuration to form stable heterotetramers. CK2 holoenzyme undergoes autophosphorylation at two serine residues (S2/S3) of its β-subunit. Recently it has been shown that CK2 α-subunits undergo intermolecular tyrosine-autophosphorylation at Y182, which may represent a specific regulatory mechanism. Also, CK2 is able to phosphorylate, under special circumstances, tyrosyl residues in proteins. CK2 is implicated in a variety of cellular functions.
350 mM NaCl, 20 mM Tris-HCl (pH 7.5 25°C), 1 mM Na2EDTA, 2 mM DTT and 0.1% Triton X-100.
a-subunit (45 kDa), b-subunit (25 kDa). The apparent molecular weight of the a-subunit estimated by SDS-PAGE is about 42 kDa.
One unit is defined as the amount of CK2 required to catalyze the transfer of 1 pmol of phosphate to CK2 Peptide Substrate, RRRADDSDDDDD (100 µM), in 1 minute at 30°C in a total reaction volume of 25 µl.
at -80°C. Avoid repeated freeze/thaw cycles.
EC 188.8.131.52; Casein Kinase II; CK2; CK II; Casein Kinase 2