ILF3抗体—艾普蒂

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     The image is immunohistochemistry of paraffin-embedded Human ovarian cancer tissue using P10014(ILF3 Antibody) at dilution 1/60. (Original magnification: ×200)    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human breast cancer tissue using P10014(ILF3 Antibody) at dilution 1/60. (Original magnification: ×200)    

  
  

Interleukin enhancer-binding factor 3 (ILF3), also known as NF90 or NFAR, is a double-stranded RNA-binding protein involved in multiple cellular processes, including RNA metabolism, transcriptional regulation, and post-transcriptional gene regulation. It exists in two major isoforms, ILF3 (NF90) and NF110. generated through alternative splicing. ILF3 interacts with RNA, DNA, and proteins, playing roles in viral response, mRNA stability, translation, and microRNA processing. It forms a heterodimer with ILF2 (NF45) to stabilize RNA interactions and modulate immune signaling pathways.

ILF3 antibodies are essential tools for studying its expression, localization, and molecular interactions. They are widely used in techniques like Western blotting, immunoprecipitation, and immunofluorescence to investigate ILF3's regulatory mechanisms in diseases, including cancer and viral infections. Dysregulation of ILF3 has been linked to tumor progression, where it may act as an oncogene by promoting cell proliferation or metastasis. In virology, ILF3 participates in host antiviral responses by binding viral RNAs or modulating interferon signaling.

Research using ILF3 antibodies also explores its role in RNA interference (RNAi) pathways and stress granule formation. These studies highlight ILF3’s dual functions in maintaining genomic stability and mediating stress responses, making it a potential therapeutic target. Validating antibody specificity is critical due to ILF3's structural similarities with other RNA-binding proteins.