Casein Kinase II (CK2)
Casein Kinase II (CKII) 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. The general recognition motif for phsophorylation by CKII is SXXE/D.
- Recombinant enzyme with no detectable protease or phosphatase contaminating activities
- Optimal activity and stability for up to 12 months
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 (1,2).
Product SourceIsolated from a strain of E. coli expressing both α and β CK2 subunits derived from a human glioblastoma cDNA library (kindly provided by Dr. D. Marshak) (3).
Recognition DeterminantThe CK2 substrate specificity is invariably determined by multiple acidic residues located at positions between -2 and +5 relative to the target amino acid (mostly Ser and rarely Thr). The general recognition motif for phsophorylation by CK2 is SXXE/D, although SXE/D and S/D, and variations of these sequences are also phosphorylated. Polyanionic compounds, like heparin, inhibit CK2 activity with a Ki of 1.4 nm (4,5).
The following reagents are supplied with this product:
Store at (°C) Concentration NEBuffer for Protein Kinases (PK) -20 10 X
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