IκB-epsilon antibodies are immunoreagents designed to detect and quantify the IkBε protein, encoded by the NFKBIE gene in humans. IkBε inhibits NF-kappa-B transcription factors by sequestering them in the cytoplasm, thereby regulating genes involved in inflammation, apoptosis, and immune responses . These antibodies are used to study IkBε's role in diseases such as cancer and autoimmune disorders.
MAB4300 detects endogenous IkBε at ~45 kDa in Western blots (WB) across multiple cell lines, including PC-3 (prostate cancer) and MCF-7 (breast cancer) .
ab230901 and ab75907 are validated for immunocytochemistry (ICC) and immunohistochemistry (IHC), enabling subcellular localization studies .
IkBε antibodies have elucidated the protein’s non-redundant role in modulating NF-kappa-B activity:
In murine B and T cells, IkBε selectively regulates c-Rel-dependent gene expression, distinct from IkBα or IkBβ .
Phospho-specific antibodies (e.g., ab75907) reveal that IkBε phosphorylation at Ser22 modulates its degradation and NF-kappa-B activation kinetics .
Neutralizing antibodies against related epsilon proteins (e.g., Clostridium perfringens epsilon toxin) demonstrate the utility of targeting pathogenic epsilon domains .
In SARS-CoV-2, cross-reactive antibodies to the Epsilon variant’s spike protein highlight challenges in viral neutralization, though these are unrelated to IkBε .
Specificity: Commercial IkBε antibodies are verified using knockout controls and peptide-blocking assays .
Storage: Lyophilized antibodies require reconstitution in sterile PBS and storage at -20°C to -70°C to prevent freeze-thaw degradation .