GART抗体;GART Antibody—艾普蒂

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     The image is immunohistochemistry of paraffin-embedded Human cervical cancer tissue using P13447(GART Antibody) at dilution 1/25. (Original magnification: ×200)    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human esophagus cancer tissue using P13447(GART Antibody) at dilution 1/25. (Original magnification: ×200)    

  
  

GART (Glycinamide Ribonucleotide Transformylase) is a key enzyme in the *de novo* purine biosynthesis pathway, catalyzing the conversion of glycinamide ribonucleotide (GAR) to formylglycinamide ribonucleotide (FGAR). This metabolic pathway is critical for DNA/RNA synthesis and cellular proliferation, making GART a potential therapeutic target in rapidly dividing cells, such as cancer cells. Dysregulation of GART has been implicated in malignancies, inflammatory diseases, and mitochondrial disorders due to its role in sustaining nucleotide pools.

GART antibodies are immunological tools developed to detect, quantify, or inhibit the enzyme’s activity in research and clinical contexts. They enable studies on GART expression patterns across tissues, its overexpression in tumors, and its interaction with chemotherapeutic agents like antifolates. In cancer research, GART antibodies help evaluate the enzyme as a biomarker for disease progression or therapeutic response. Additionally, they are used to explore GART inhibition strategies aimed at starving cancer cells of nucleotides, thereby inducing apoptosis.

Recent advances in antibody engineering have improved GART-specific monoclonal antibodies for diagnostic assays and preclinical drug development. However, challenges remain in balancing target specificity and minimizing off-effects in complex biological systems. Ongoing studies continue to elucidate GART's broader roles in cellular metabolism and disease pathogenesis.