The Inhibitor of Nuclear Factor Kappa-B Kinase (IKK) is a pivotal serine/threonine kinase complex that plays a crucial role in regulating the Nuclear Factor Kappa-B (NF-κB) signaling pathway. This pathway is fundamental for controlling diverse physiological and pathological processes, including immune responses, inflammation, cell proliferation, and apoptosis. The IKK complex comprises three main subunits: IKKα (also known as IKK1), IKKβ (IKK2), and IKKγ (or NEMO/IKBKG). Each subunit contributes uniquely to the complex's structure and function. IKKα possesses kinase activity, albeit lower than IKKβ. Its precise role in NF-κB activation remains somewhat elusive, but it may be involved in specific types of NF-κB activation. IKKβ serves as the primary kinase subunit within the complex, exhibiting robust kinase activity. IKKβ is essential for activating the NF-κB pathway by phosphorylating the inhibitory protein IκB, leading to its degradation and subsequent release of NF-κB for nuclear translocation and transcriptional activation. IKK's primary function lies in the activation of the NF-κB signaling pathway. By phosphorylating specific serine residues on the IκB proteins, IKK triggers their ubiquitination and subsequent degradation by the proteasome. This process frees NF-κB from inhibition, allowing it to translocate to the nucleus and activate the transcription of target genes.