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     Western blot analysis of Golgin 97 expression in HeLa cell lysate.    

  
  

Golgin97 is a peripheral membrane protein predominantly localized to the trans-Golgi network (TGN), where it plays a critical role in maintaining Golgi structure, vesicle trafficking, and cargo sorting. As a member of the golgin family, it contains a conserved GRIP domain at its C-terminus, which mediates its attachment to the TGN through interactions with Arl1 and Rab6 GTPases. Golgin97 is involved in retrograde transport of endosomal vesicles to the Golgi and regulates the recycling of proteins like the mannose-6-phosphate receptor.

Antibodies targeting Golgin97 are widely used as markers for the TGN in immunofluorescence and immunoblotting experiments. These antibodies help researchers study Golgi organization, vesicular transport mechanisms, and dysfunctions linked to diseases such as cancer, neurodegenerative disorders, and viral infections that exploit Golgi-dependent pathways.

The Golgin97 antibody is typically raised in rabbits or mice using immunogenic peptides or recombinant protein fragments. Specificity is validated via knockout cell lines or siRNA-mediated depletion. Commercial antibodies often cross-react with homologs like Golgin245 (human) or GCC88 (mouse), necessitating careful experimental controls. Its role in TGN integrity and membrane trafficking continues to make Golgin97 a key focus in cell biology and pathology research.