TRIM23抗体

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     The image is immunohistochemistry of paraffin-embedded Human esophagus cancer tissue using P12291(TRIM23 Antibody) at dilution 1/25. (Original magnification: ×200)    

  
  

The TRIM23 antibody is a tool used to detect and study TRIM23 (Tripartite Motif-containing protein 23), a member of the TRIM family of proteins involved in diverse cellular processes, including innate immunity, autophagy, and antiviral responses. TRIM23 contains characteristic domains: a RING finger, B-box, and coiled-coil regions, along with a unique GTP-binding domain (ARF-type), distinguishing it from other TRIM proteins. It functions as an E3 ubiquitin ligase, mediating protein ubiquitination to regulate signaling pathways. Research highlights its role in modulating NF-κB activation, promoting autophagy through interactions with autophagy-related proteins, and participating in antiviral defense by targeting viral components for degradation.

TRIM23 antibodies are widely employed in techniques like Western blotting, immunoprecipitation, and immunofluorescence to investigate its expression, localization (primarily cytoplasmic), and interactions in cell lines or tissues. These antibodies are critical in studies linking TRIM23 to diseases such as neurodegenerative disorders and cancer, where dysregulated TRIM23 expression or activity may contribute to pathogenesis. Commercial TRIM23 antibodies are typically raised in rabbits or mice, with validation data confirming specificity for human, mouse, or rat isoforms. Researchers rely on these antibodies to explore TRIM23's dual enzymatic roles (ubiquitination and GTPase activity) and its crosstalk with pathways like Arf6-mediated membrane trafficking, underscoring its multifaceted regulatory functions in cellular homeostasis and disease.