PPAT抗体;PPAT Antibody—艾普蒂

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     Gel: 10%SDS-PAGE, Lysate: 40 μg, Lane 1-5: Hela cells, Raji cells, Jurkat cells, A549 cells, NIH/3T3 cells, Primary antibody: P08373(PPAT Antibody) at dilution 1/250, Secondary antibody: Goat anti rabbit IgG at 1/8000 dilution, Exposure time: 20 seconds    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human cervical cancer tissue using P08373(PPAT Antibody) at dilution 1/50. (Original magnification: ×200)    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human brain  tissue using P08373(PPAT Antibody) at dilution 1/50. (Original magnification: ×200)    

  
  

PPAT (Phosphoribosyl Pyrophosphate Amidotransferase) is a rate-limiting enzyme in the *de novo* purine biosynthesis pathway, catalyzing the first committed step of converting phosphoribosyl pyrophosphate (PRPP) into phosphoribosylamine. This enzyme plays a critical role in nucleotide metabolism, making it essential for cellular proliferation, DNA/RNA synthesis, and energy homeostasis. Dysregulation of PPAT has been linked to various pathologies, including cancer, where rapidly dividing cells rely heavily on upregulated purine synthesis. Its overexpression in tumors, such as glioblastoma and leukemia, highlights its potential as a therapeutic target.

PPAT antibodies are tools developed to detect, quantify, or inhibit PPAT protein expression in research and diagnostic contexts. These antibodies enable studies on PPAT’s spatial-temporal expression, interaction partners, and regulatory mechanisms. In drug discovery, PPAT inhibitors (e.g., antifolates) are explored for chemotherapy, and antibodies aid in validating target engagement or monitoring therapeutic efficacy. Additionally, PPAT antibodies contribute to understanding metabolic disorders tied to purine imbalance, such as Lesch-Nyhan syndrome. Most PPAT antibodies are raised against conserved epitopes in human or murine PPAT, with applications in Western blotting, immunohistochemistry, and ELISA. Challenges include ensuring specificity due to structural similarities with other amidotransferases. Ongoing research focuses on optimizing antibody performance for precision in complex biological samples.