RPAP3抗体

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     Gel: 10%SDS-PAGE, Lysate: 40 μg, Lane: Mouse kidney tissue, Primary antibody: P07616(RPAP3 Antibody) at dilution 1/400, Secondary antibody: Goat anti rabbit IgG at 1/8000 dilution, Exposure time: 1 minute    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human brain tissue using P07616(RPAP3 Antibody) at dilution 1/20. (Original magnification: ×200)    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human lung cancer tissue using P07616(RPAP3 Antibody) at dilution 1/20. (Original magnification: ×200)    

  
  

The RNA polymerase II-associated protein 3 (RPAP3) is a conserved eukaryotic protein involved in transcriptional regulation and chaperone-mediated assembly of macromolecular complexes. It is a key component of the R2TP (RUVBL1/RUVBL2-RPAP3-PIH1D1) complex, which facilitates the assembly of RNA polymerase II, snoRNPs, and phosphatidylinositol 3-kinase-related kinases (PIKKs). RPAP3 contains tetratricopeptide repeat (TPR) domains that mediate interactions with heat shock proteins (HSP90) and other client proteins, playing a critical role in stress response and cellular homeostasis.

Antibodies targeting RPAP3 are essential tools for studying its function in transcription, DNA damage repair, and ribosome biogenesis. They are widely used in techniques like immunoprecipitation, Western blotting, and immunofluorescence to investigate RPAP3’s localization, protein interactions, and expression levels. Research has linked RPAP3 dysregulation to cancers, neurodegenerative disorders, and ciliopathies, making these antibodies valuable in disease mechanism studies. For example, RPAP3 overexpression in certain tumors correlates with poor prognosis, suggesting its role in oncogenic pathways. Additionally, RPAP3 antibodies help dissect R2TP complex dynamics, aiding the development of therapies targeting chaperone-mediated processes. Validation of antibody specificity via knockout controls is critical due to RPAP3’s structural homology with other TPR-containing proteins.