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     The image is immunohistochemistry of paraffin-embedded Human cervical cancer tissue using P06034(UNC93B1 Antibody) at dilution 1/35. (Original magnification: ×200)    

  
  

UNC93B1 is a transmembrane protein primarily localized in the endoplasmic reticulum and endolysosomal compartments, playing a critical role in regulating the trafficking and activation of endosomal Toll-like receptors (TLRs), particularly TLR3. TLR7. TLR8. and TLR9. These TLRs are essential for detecting microbial nucleic acids and initiating innate immune responses. UNC93B1 binds directly to these TLRs, facilitating their transport from the endoplasmic reticulum to endosomes and ensuring their proper signaling function. Mutations in UNC93B1 have been linked to impaired TLR signaling, increasing susceptibility to viral infections (e.g., herpes simplex encephalitis) and altering autoimmune disease progression.

Antibodies targeting UNC93B1 are vital tools for studying its expression, localization, and interaction with TLRs. They are widely used in techniques like Western blotting, immunoprecipitation, immunofluorescence, and flow cytometry to assess protein levels in immune cells or tissues. Such antibodies help elucidate UNC93B1’s regulatory mechanisms in TLR-mediated immune responses and its role in pathologies, including infections, autoimmune disorders (e.g., systemic lupus erythematosus), and inflammatory diseases. Commercially available UNC93B1 antibodies are often validated in knockout models to ensure specificity. Research using these antibodies has advanced understanding of how UNC93B1 dysfunction contributes to immune dysregulation, offering potential therapeutic targets for modulating excessive TLR signaling.