RAB9A抗体—艾普蒂

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     Gel: 12%SDS-PAGE, Lysate: 40 μg, Lane 1-3: RAW264.7, hepg2 cells, hela cells, Primary antibody: P08665(RAB9A Antibody) at dilution 1/300, 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 breast cancer tissue using P08665(RAB9A Antibody) at dilution 1/25. (Original magnification: ×200)    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human brain  tissue using P08665(RAB9A Antibody) at dilution 1/25. (Original magnification: ×200)    

  
  

The RAB9A antibody is a crucial tool in studying the RAB9A protein, a member of the Ras-associated binding (RAB) GTPase family involved in intracellular membrane trafficking. RAB9A primarily regulates vesicular transport between late endosomes and the trans-Golgi network, playing a key role in endosomal-lysosomal processing, lipid metabolism, and autophagy. It is also implicated in the biogenesis of lysosome-related organelles and the recycling of mannose-6-phosphate receptors for lysosomal enzyme sorting. Dysregulation of RAB9A has been linked to inherited disorders like Charcot-Marie-Tooth disease and cancers, where altered vesicular trafficking contributes to tumor progression.

RAB9A antibodies are widely used in research to detect and localize the protein via techniques such as Western blotting, immunofluorescence, and immunohistochemistry. These antibodies help elucidate RAB9A’s functional interactions, post-translational modifications, and expression patterns under varying cellular conditions. Many commercially available RAB9A antibodies are monoclonal or polyclonal, raised in hosts like rabbits or mice, and validated for specificity against conserved epitopes. Their applications extend to studying viral pathogenesis (e.g., rabies virus exploitation of RAB pathways) and neurodegenerative diseases marked by lysosomal dysfunction. As RAB9A gains attention as a potential therapeutic target or biomarker, its antibodies remain vital for advancing mechanistic insights into membrane trafficking disorders.