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     Western blot analysis of Phospho-NF-KB p65 (Ser536) in various lysates using Phospho-NF-KB p65 (Ser536) antibody.    

  
  

The Phospho-NF-κB p65 (Ser536) antibody is a critical tool for studying the activation status of the NF-κB signaling pathway, which plays a central role in regulating immune responses, inflammation, cell survival, and apoptosis. NF-κB is a transcription factor composed of homo- or heterodimers of Rel family proteins, with p65 (RelA) being a major subunit. In resting cells, NF-κB is sequestered in the cytoplasm by inhibitory IκB proteins. Upon stimulation by cytokines, pathogens, or stress, IκB is degraded, allowing NF-κB to translocate to the nucleus and activate target genes. Phosphorylation of p65 at Ser536. mediated by kinases such as IKKβ, RSK1. or AKT, enhances its transcriptional activity by promoting nuclear localization, DNA binding, and interaction with coactivators. This post-translational modification is a hallmark of canonical NF-κB pathway activation.

The Phospho-NF-κB p65 (Ser536) antibody specifically detects this phosphorylation event, enabling researchers to assess pathway activation in diseases like cancer, autoimmune disorders, and chronic inflammation. It is widely used in techniques including Western blotting, immunohistochemistry, and immunofluorescence to study cellular responses to stimuli such as TNF-α, IL-1β, or LPS. Dysregulation of Ser536 phosphorylation has been linked to tumor progression, resistance to therapy, and inflammatory conditions, making this antibody valuable for both basic research and drug development targeting NF-κB signaling.