CK2 alpha/CSNK2A2 Protein, Human (sf9, His-GST)

CSNK2A2, the catalytic subunit of a constitutively active serine/threonine-protein kinase complex, plays a pivotal role in phosphorylating a diverse array of substrates with acidic residues located C-terminal to the phosphorylated serine or threonine. This versatile protein regulator is involved in regulating critical cellular processes, including cell cycle progression, apoptosis, and transcription, as well as influencing viral infection. Acting as a central regulatory node, CSNK2A2 integrates and coordinates various signals, orchestrating an appropriate cellular response. During mitosis, it functions within the p53/TP53-dependent spindle assembly checkpoint, preserving cyclin-B-CDK1 activity and inducing G2 arrest in response to spindle damage. Furthermore, CSNK2A2 is essential for p53/TP53-mediated apoptosis, phosphorylating 'Ser-392' of p53/TP53 after UV irradiation, and it exerts a negative regulatory effect on apoptosis. Notably, CSNK2A2 displays a broad impact on cellular signaling, phosphorylating caspases, apoptotic regulator NOL3, RNA polymerases, and numerous transcription factors. Its influence extends to molecular chaperones, such as Hsp90 and its co-chaperones, highlighting its essential role in chaperone function. Additionally, CSNK2A2 regulates Wnt signaling, acts as an ectokinase for extracellular proteins, and exerts its influence during viral infection by phosphorylating proteins involved in the life cycles of various viruses, underscoring its multifaceted and crucial role in cellular homeostasis.