TRIM38抗体;TRIM38 Antibody—艾普蒂

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     The image is immunohistochemistry of paraffin-embedded Human esophagus cancer tissue using P13759(TRIM38 Antibody) at dilution 1/50. (Original magnification: ×200)    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human liver cancer tissue using P13759(TRIM38 Antibody) at dilution 1/50. (Original magnification: ×200)    

  
  

**Background of TRIM38 Antibody**

TRIM38 is a member of the tripartite motif (TRIM) protein family, characterized by its conserved RING, B-box, and coiled-coil domains. It functions as an E3 ubiquitin ligase, playing roles in regulating innate immune responses, inflammation, and antiviral defense. TRIM38 modulates signaling pathways such as NF-κB and type I interferon (IFN) by targeting proteins like TAK1. STING, and TRAF6 for ubiquitination, influencing their stability or activity. Studies highlight its dual regulatory effects—promoting or inhibiting immune signaling depending on cellular context.

Antibodies against TRIM38 are essential tools for investigating its expression, localization, and molecular interactions. They enable detection of endogenous TRIM38 in techniques like Western blotting, immunoprecipitation, and immunofluorescence. TRIM38’s subcellular distribution (cytoplasmic or nuclear) and tissue-specific expression patterns, particularly in immune cells, make its antibody valuable for studying immune regulation and disease mechanisms.

Research using TRIM38 antibodies has linked the protein to autoimmune disorders, viral infections, and cancer, underscoring its therapeutic potential. Validated antibodies with high specificity are critical, as TRIM38 shares structural homology with other TRIM proteins. Both monoclonal and polyclonal variants are available, tailored for different experimental needs. Overall, TRIM38 antibodies facilitate deeper insights into its multifaceted roles in cellular homeostasis and pathogen response.