TRIM40抗体

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     The image is immunohistochemistry of paraffin-embedded Human liver cancer tissue using P05233(TRIM40 Antibody) at dilution 1/40. (Original magnification: ×200)    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human thyroid cancer tissue using P05233(TRIM40 Antibody) at dilution 1/40. (Original magnification: ×200)    

  
  

The TRIM40 antibody is a research tool designed to detect and study TRIM40 (Tripartite Motif-containing protein 40), a member of the TRIM family known for its roles in ubiquitination, innate immunity, and cancer regulation. TRIM40 contains a conserved N-terminal TRIM motif (RING, B-box, and coiled-coil domains) and a C-terminal PRY-SPRY domain, which may mediate protein-protein interactions. Functionally, TRIM40 acts as an E3 ubiquitin ligase, promoting proteasomal degradation of target proteins through ubiquitination. Studies suggest it regulates inflammatory signaling pathways (e.g., NF-κB) and may act as a tumor suppressor in certain cancers by targeting oncoproteins for degradation. For instance, TRIM40 has been reported to be downregulated in hepatocellular carcinoma and colorectal cancer, correlating with poor prognosis.

The antibody is typically generated using recombinant TRIM40 protein or synthetic peptides as immunogens, often in hosts like rabbits or mice. It enables detection of endogenous TRIM40 in applications such as Western blotting, immunofluorescence, and immunoprecipitation. Validation usually includes knockout cell lines or siRNA-mediated silencing to confirm specificity. Researchers use TRIM40 antibodies to explore its expression patterns, subcellular localization (e.g., cytoplasmic or nuclear), and interactions with signaling molecules. Recent interest focuses on its role in autoimmune diseases, viral infection responses, and cancer progression, making it a potential biomarker or therapeutic target. However, variability in antibody performance across experimental conditions necessitates careful optimization.