NRIP3抗体—艾普蒂 新品

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     Black line: Control Antigen (100 ng); Purple line: Antigen(10ng); Blue line: Antigen (50 ng); Red line: Antigen (100 ng);    

  
  

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     Western blot analysis using PTPRC mouse mAb against Hela (1) and A431 (2) cell lysate.    

  
  

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     Immunohistochemical analysis of paraffin-embedded human colon cancer tissues using PTPRC mouse mAb with DAB staining.    

  
  

The nuclear receptor-interacting protein 3 (NRIP3), also known as receptor-interacting protein 140 (RIP140), is a transcriptional coregulator that modulates the activity of nuclear receptors and other transcription factors. Initially identified for its role in estrogen receptor (ER) signaling, NRIP3 is involved in diverse cellular processes, including metabolism, inflammation, and cancer progression. It functions as a scaffold protein, recruiting histone deacetylases (HDACs) and other chromatin-modifying enzymes to repress or enhance target gene expression, depending on cellular context. Structurally, NRIP3 contains multiple receptor interaction domains and motifs that facilitate binding to ligand-activated nuclear receptors, such as ER, thyroid hormone receptor (TR), and peroxisome proliferator-activated receptors (PPARs).

Antibodies targeting NRIP3 are essential tools for studying its expression, localization, and molecular interactions. They are widely used in techniques like Western blotting, immunohistochemistry (IHC), and chromatin immunoprecipitation (ChIP) to investigate its role in hormone-dependent pathways, metabolic regulation, and disease mechanisms. Dysregulation of NRIP3 has been linked to conditions such as breast cancer, ovarian cancer, and metabolic syndrome, making it a potential therapeutic target. Research utilizing NRIP3 antibodies has helped clarify its dual role as both a coactivator and corepressor, highlighting context-dependent functions in cellular homeostasis. These antibodies also aid in exploring post-translational modifications (e.g., phosphorylation) that regulate NRIP3 activity.