GMDS抗体—艾普蒂

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     The image is immunohistochemistry of paraffin-embedded Human tonsil tissue using P10125(GMDS Antibody) at dilution 1/70. (Original magnification: ×200)    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human cervical cancer tissue using P10125(GMDS Antibody) at dilution 1/70. (Original magnification: ×200)    

  
  

GMDS (GDP-mannose 4.6-dehydratase) is a key enzyme in the biosynthesis of fucose, a sugar critical for protein glycosylation. It catalyzes the conversion of GDP-mannose to GDP-4-keto-6-deoxymannose, a precursor for GDP-fucose, which is essential for post-translational modification of glycoproteins and glycolipids. Fucosylated molecules play vital roles in cell adhesion, immune response, and signal transduction. Dysregulation of GMDS has been implicated in cancer metastasis, inflammation, and autoimmune disorders due to altered fucosylation patterns affecting cell-cell interactions or immune recognition.

GMDS antibodies are tools used to study the enzyme's expression, localization, and function in biological systems. They are critical in detecting GMDS protein levels in tissues or cell lines, often applied in techniques like Western blot, immunohistochemistry, or flow cytometry. Such antibodies help explore GMDS-related pathways in diseases; for example, reduced GMDS expression in certain cancers correlates with poor prognosis. Researchers also utilize GMDS antibodies to validate gene knockout models or assess therapeutic interventions targeting fucose metabolism. Commercially available GMDS antibodies are typically raised against specific epitopes, with validation in cross-reactivity (human, mouse, rat) and application-specific contexts. Their development supports both basic research and potential diagnostic applications, particularly in understanding glycosylation disorders.