RNF128抗体—艾普蒂

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     The image is immunohistochemistry of paraffin-embedded Human colorectal cancer tissue using P08713(RNF128 Antibody) at dilution 1/110. (Original magnification: ×200)    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human tonsil tissue using P08713(RNF128 Antibody) at dilution 1/110. (Original magnification: ×200)    

  
  

RNF128. also known as GRAIL (gene related to anergy in lymphocytes), is an E3 ubiquitin ligase belonging to the RING finger protein family. It plays a critical role in immune regulation, particularly in T-cell activation and tolerance. RNF128 mediates ubiquitination-dependent processes that promote T-cell anergy or apoptosis by targeting key signaling molecules like protein kinase C-theta (PKCθ) and CD28 for degradation. This activity dampens T-cell receptor (TCR) signaling, contributing to peripheral immune tolerance and preventing autoimmune responses. Dysregulation of RNF128 has been implicated in autoimmune diseases, cancer immune evasion, and chronic infections.

RNF128 antibodies are essential tools for studying its expression, function, and interaction networks. They are widely used in techniques such as Western blotting, immunoprecipitation, immunohistochemistry (IHC), and flow cytometry to investigate RNF128's role in T-cell biology and disease contexts. Specific monoclonal or polyclonal antibodies help identify post-translational modifications, subcellular localization, and tissue-specific expression patterns. Research utilizing RNF128 antibodies has revealed its dual role as both a tumor suppressor and an immune checkpoint regulator, highlighting its therapeutic potential in cancer immunotherapy and autoimmune disorders. Validated antibodies ensure specificity for distinguishing RNF128 isoforms and quantifying expression changes in experimental or clinical samples.