RNaseL抗体;RNaseL Antibody—艾普蒂

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     Western blot analysis of RNase L expression in THP1 cell lysate.    

  
  

RNaseL (ribonuclease L) is a critical enzyme in innate immunity, primarily activated during antiviral responses. It is part of the interferon (IFN) pathway, where its activity is regulated by 2',5'-oligoadenylates (2-5A) synthesized by oligoadenylate synthetases (OAS) upon viral RNA detection. Binding of 2-5A triggers RNaseL dimerization, enabling its endoribonuclease function to degrade viral and cellular single-stranded RNAs, thereby inhibiting viral replication and inducing apoptosis in infected cells. Dysregulation of RNaseL has been linked to chronic inflammatory diseases, cancer, and susceptibility to viral infections.

RNaseL antibodies are essential tools for studying its expression, activation, and role in immune regulation. These antibodies enable detection of RNaseL protein levels, cellular localization (cytosolic and nuclear), and post-translational modifications via techniques like Western blotting, immunohistochemistry, and immunofluorescence. Monoclonal antibodies offer high specificity, while polyclonal antibodies may detect multiple epitopes, aiding in diverse experimental setups. Validated RNaseL antibodies help investigate its involvement in antiviral defense, apoptosis, and tumor suppression, as well as its interaction with viral evasion proteins. Research using these antibodies has also explored RNaseL's association with prostate cancer risk and chronic fatigue syndrome (CFS/ME), highlighting its broader physiological impact beyond innate immunity. Proper antibody validation, including knockout controls, is crucial to ensure specificity in experimental models.