TRIM39抗体—艾普蒂

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     Gel: 8%SDS-PAGE, Lysate: 40 μg, Lane: Mouse skeletal muscle tissue lysate, Primary antibody: P09556(TRIM39 Antibody) at dilution 1/200, Secondary antibody: Goat anti rabbit IgG at 1/8000 dilution, Exposure time: 3 seconds    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human liver cancer tissue using P09556(TRIM39 Antibody) at dilution 1/20. (Original magnification: ×200)    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human gastric cancer tissue using P09556(TRIM39 Antibody) at dilution 1/20. (Original magnification: ×200)    

  
  

TRIM39 (Tripartite Motif-Containing Protein 39) is a member of the TRIM protein family, characterized by conserved RING, B-box, and coiled-coil domains. It functions as an E3 ubiquitin ligase, playing roles in ubiquitination-mediated protein degradation and signaling regulation. TRIM39 is involved in diverse cellular processes, including cell cycle progression, apoptosis, DNA damage response, and immune regulation. Studies suggest it interacts with proteins like CDK1/cyclin B1 to influence mitotic entry and with p53 to modulate apoptosis. Its role in cancer is context-dependent, acting as a tumor suppressor in some contexts by promoting apoptosis or cell cycle arrest, while potentially supporting tumor survival in others through stress adaptation pathways.

TRIM39 antibodies are essential tools for detecting TRIM39 expression in research applications such as Western blotting, immunohistochemistry, and immunofluorescence. They help elucidate TRIM39’s tissue-specific expression patterns, subcellular localization (primarily nuclear), and regulatory mechanisms. Recent interest focuses on its potential as a therapeutic target, particularly in cancers with dysregulated ubiquitination pathways. Commercial TRIM39 antibodies are typically validated for specificity using knockout cell lines or siRNA-mediated knockdown. Researchers should verify antibody cross-reactivity with homologous TRIM family members, as sequence similarities may lead to off-target detection.