CK2 exists as a tetrameric complex composed of two catalytic subunits (alpha and alpha’) and two regulatory beta subunits . The alpha and alpha’ subunits are catalytically identical but differ in their regulatory interactions. The alpha’ subunit, also known as CK2 Alpha 2 Prime (CSNK2A2), is one of the catalytic subunits of this enzyme .
CK2 is involved in the phosphorylation of a wide range of substrates, including key intracellular signaling proteins implicated in tumor suppression (e.g., p53 and PTEN) and tumorigenesis (e.g., myc, jun, NF-kappaB) . It also influences Wnt signaling via beta-catenin phosphorylation and the PI 3-K signaling pathway via the phosphorylation of Akt .
The recombinant form of CK2 Alpha 2 Prime (Human) is produced using various expression systems, such as insect cells or HEK293T cells . The recombinant protein is often tagged (e.g., GST-tag) to facilitate purification and detection . It is typically stored in a buffer containing tris, DTT, NaCl, EDTA, Triton X-100, and glycerol to maintain stability .
Deregulation of CK2 has been linked to various diseases, including cancer. The enzyme’s ability to phosphorylate tumor suppressor proteins and proteins involved in cell survival pathways makes it a potential target for cancer therapy . Additionally, CK2’s role in DNA repair and response to UV irradiation-induced DNA damage further underscores its importance in maintaining cellular integrity .