PNPO抗体;PNPO Antibody—艾普蒂

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     Gel: 8%SDS-PAGE, Lysate: 40 μg, Lane 1-4: Human fetal brain tissue, PC-3, Hela and 293T cell lysates, Primary antibody: P13186(PNPO Antibody) at dilution 1/700, Secondary antibody: Goat anti rabbit IgG at 1/8000 dilution, Exposure time: 30 seconds    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human brain tissue using P13186(PNPO Antibody) at dilution 1/30. (Original magnification: ×200)    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human gastric cancer tissue using P13186(PNPO Antibody) at dilution 1/30. (Original magnification: ×200)    

  
  

Pyridoxamine 5'-phosphate oxidase (PNPO) is a critical enzyme in vitamin B6 metabolism, responsible for converting pyridoxamine 5'-phosphate (PMP) and pyridoxine 5'-phosphate (PNP) into pyridoxal 5'-phosphate (PLP), the active coenzyme form essential for neurotransmitter synthesis, amino acid metabolism, and heme biosynthesis. PNPO antibodies are immunological tools developed to detect and study the expression, localization, and function of this enzyme in biological systems.

Research on PNPO antibodies has gained prominence due to their role in investigating PNPO deficiency, a rare autosomal recessive disorder linked to mutations in the PNPO gene. This condition disrupts PLP production, leading to severe neonatal epileptic encephalopathy and other neurological impairments. PNPO antibodies enable the detection of reduced enzyme levels or abnormal protein variants in patient samples, aiding in diagnostics and mechanistic studies.

Additionally, these antibodies are utilized in preclinical research to explore PNPO's tissue-specific expression, regulation under metabolic stress, and interactions with other B6 vitamers. They are critical in Western blotting, immunohistochemistry, and ELISA assays, helping to elucidate PNPO's role in developmental biology, neurological health, and potential therapeutic strategies for vitamin B6-dependent disorders. The development of high-specificity PNPO antibodies remains vital for advancing both clinical and molecular understanding of this enzyme.