UAP1抗体—艾普蒂

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     Gel: 6%SDS-PAGE, Lysate: 40 μg, Lane: Human testis tissue lysate, Primary antibody: P09295(UAP1 Antibody) at dilution 1/250, 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 tonsil tissue using P09295(UAP1 Antibody) at dilution 1/30. (Original magnification: ×200)    

  
  

The UAP1 antibody targets the enzyme UDP-N-acetylglucosamine pyrophosphorylase 1 (UAP1), a key player in the hexosamine biosynthesis pathway (HBP). UAP1 catalyzes the conversion of glucosamine-6-phosphate and UTP into UDP-N-acetylglucosamine (UDP-GlcNAc), a critical substrate for protein O-GlcNAcylation and glycosylation processes. These post-translational modifications regulate diverse cellular functions, including nutrient sensing, stress response, and signal transduction. Dysregulation of UAP1 and UDP-GlcNAc levels has been implicated in metabolic disorders, cancer, and neurodegenerative diseases.

UAP1 antibodies are widely used in research to study the enzyme’s expression, localization, and interaction networks. They enable detection of UAP1 via techniques like Western blotting, immunofluorescence, and immunohistochemistry. Such studies have linked UAP1 overexpression to cancer progression, particularly in tumors reliant on enhanced glycosylation for growth and metastasis. Additionally, UAP1 antibodies aid in exploring the enzyme’s role in diabetes, where altered O-GlcNAcylation impacts insulin signaling. As interest in metabolic reprogramming and glycosylation expands, UAP1 antibodies remain vital tools for dissecting HBP-related mechanisms in health and disease. Commercial variants vary in specificity, requiring validation for cross-reactivity with homologous enzymes like UAP2.