The Phospho-IKK alpha/beta (Ser176/Ser177) antibody detects the activated form of the inhibitor of nuclear factor kappa-B kinase (IKK) complex, a central regulator of the NF-κB signaling pathway. The IKK complex, composed of catalytic subunits IKKα (IKK1) and IKKβ (IKK2) along with the regulatory scaffold protein NEMO (IKKγ), plays a critical role in inflammatory, immune, and stress responses. Activation of the complex occurs through phosphorylation of specific serine residues (Ser176 in IKKα and Ser177 in IKKβ) within their activation loops. This phosphorylation event, often triggered by pro-inflammatory cytokines (e.g., TNF-α, IL-1) or pathogen-associated molecular patterns, enables the IKK complex to phosphorylate the inhibitor of NF-κB (IκB), marking it for proteasomal degradation. Subsequent NF-κB nuclear translocation initiates transcription of target genes involved in inflammation, cell survival, and proliferation.
The Phospho-IKK alpha/beta (Ser176/Ser177) antibody is widely used in research to study NF-κB pathway activation under various conditions, such as infection, autoimmune disorders, or cancer. It specifically recognizes the phosphorylated state of IKKα/β, distinguishing active from inactive kinase forms. Applications include Western blotting, immunofluorescence, and immunohistochemistry to assess pathway activity in cell lines, tissues, or disease models. Its utility extends to drug discovery, where it helps evaluate compounds targeting IKK or upstream regulators. Validated in multiple experimental systems, this antibody is essential for elucidating mechanisms linking IKK activation to pathologies like chronic inflammation, neurodegeneration, and tumor progression.