DDOST抗体—艾普蒂

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     Gel: 8%SDS-PAGE, Lysate: 40 μg, Lane 1-3: A172, HepG2 and LOVO cell lysates, Primary antibody: P09599(DDOST Antibody) at dilution 1/200, Secondary antibody: Goat anti rabbit IgG at 1/8000 dilution, Exposure time: 5 seconds    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human liver cancer tissue using P09599(DDOST Antibody) at dilution 1/20. (Original magnification: ×200)    

  
  

DDOST (dolichyl-diphosphooligosaccharide-protein glycosyltransferase) is a critical enzyme in the oligosaccharyltransferase (OST) complex, which mediates the central step of N-linked glycosylation in the endoplasmic reticulum. This post-translational modification is essential for protein folding, quality control, and cellular trafficking. DDOST, also known as ribophorin II, anchors the catalytic STT3 subunit to the ER membrane, ensuring proper recognition and transfer of oligosaccharides to nascent polypeptides.

Antibodies targeting DDOST are valuable tools for studying N-glycosylation mechanisms and associated diseases. Mutations in DDOST have been linked to congenital disorders of glycosylation (CDGs), characterized by multisystemic abnormalities. Researchers use DDOST antibodies in techniques like Western blotting, immunofluorescence, and immunoprecipitation to investigate its expression, localization, and interactions within the OST complex.

Additionally, DDOST dysregulation has been implicated in cancer, neurodegeneration, and immune disorders, making these antibodies relevant for biomarker discovery and therapeutic development. Their specificity enables differentiation between functional OST isoforms and aids in elucidating tissue-specific glycosylation pathways. Overall, DDOST antibodies serve as key reagents for advancing glycobiology research and understanding diseases rooted in protein glycosylation defects.