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     The image is immunohistochemistry of paraffin-embedded Human liver cancer tissue using P01968(UBL3 Antibody) at dilution 1/30. (Original magnification: ×200)    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human breast cancer tissue using P01968(UBL3 Antibody) at dilution 1/30. (Original magnification: ×200)    

  
  

Ubiquitin-like protein 3 (UBL3), also known as membrane-anchored ubiquitin-fold protein (MUB), is a small (~12 kDa) post-translationally modified protein belonging to the ubiquitin-like family. Unlike ubiquitin, UBL3 lacks a C-terminal diglycine motif required for canonical ubiquitination but contains a conserved C-terminal prenylation site (CAAX box) that enables its attachment to cellular membranes via farnesylation. UBL3 is implicated in membrane trafficking, protein sorting, and the regulation of cell surface receptor internalization. It interacts with ESCRT (Endosomal Sorting Complex Required for Transport) machinery and may modulate vesicular transport or viral budding processes.

Antibodies targeting UBL3 are critical tools for studying its localization, interactions, and roles in cellular processes. These antibodies are typically validated for applications such as Western blotting, immunofluorescence, and immunoprecipitation. Research suggests UBL3 participates in neurodegenerative diseases and cancer, with altered expression observed in conditions like Alzheimer’s disease and certain carcinomas. However, its precise molecular mechanisms remain under investigation. Commercially available UBL3 antibodies are often raised against conserved regions (e.g., N-terminal residues 1-50) and require validation using knockout cell lines or siRNA-mediated knockdown to confirm specificity. Understanding UBL3's function through antibody-based assays may shed light on its involvement in membrane dynamics and disease pathways.