POMK抗体—艾普蒂

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     Gel: 8%SDS-PAGE, Lysate: 40 μg, Lane: TM4 cell, Primary antibody: P09084(POMK Antibody) at dilution 1/350, Secondary antibody: Goat anti rabbit IgG at 1/8000 dilution, Exposure time: 15 seconds    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human brain tissue using P09084(POMK Antibody) at dilution 1/25. (Original magnification: ×200)    

  
  

POMK (Protein O-Mannose Kinase), also known as SGK196. is an enzyme encoded by the *POMK* gene in humans. It plays a critical role in the post-translational modification of α-dystroglycan (α-DG), a key component of the dystrophin-glycoprotein complex (DGC) that stabilizes muscle and neuronal cell membranes. Specifically, POMK phosphorylates O-mannose residues on α-DG, a step essential for its functional glycosylation. This glycosylation enables α-DG to bind extracellular matrix proteins like laminin, maintaining structural integrity in tissues such as skeletal muscle, the brain, and the retina.

Antibodies targeting POMK are vital tools for studying its expression, localization, and function in both physiological and pathological contexts. They are widely used in techniques like Western blotting, immunohistochemistry, and immunofluorescence to investigate POMK-related mechanisms in diseases. Mutations in *POMK* are linked to congenital muscular dystrophies (e.g., Walker-Warburg syndrome and Limb-Girdle Muscular Dystrophy), often characterized by defective α-DG glycosylation, muscle degeneration, and neurological abnormalities. POMK antibodies help identify these mutations, aiding in diagnostics and research into therapeutic strategies, such as gene therapy or enzyme replacement. Additionally, they contribute to exploring POMK's roles beyond muscular disorders, including potential involvement in cancer or neurological conditions. As research progresses, POMK antibodies remain crucial for unraveling the molecular basis of glycosylation-related pathologies.