Under an unstimulated condition, the inhibitor of NF-κB proteins (IκBs), including mainly IκBα, IκBβ, and IκBε, retain inactive NF-κB dimmers in the cytosol, whereas in response to various extracellular stimuli, including infection, proinflammatory cytokines, and antigen receptor engagement, the activated IκB kinase complexes phosphorylate IκB proteins, resulting in their ubiquitination and proteasomal degradation and consequently inducing the release of NF-κB for nuclear translocation and the activation of target gene transcription [6, 105]. This evidence concerns the gene NFKB1 and infection.