UBD抗体—艾普蒂

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     The image is immunohistochemistry of paraffin-embedded Human tonsil tissue using P10016(UBD Antibody) at dilution 1/50. (Original magnification: ×200)    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human lung cancer tissue using P10016(UBD Antibody) at dilution 1/50. (Original magnification: ×200)    

  
  

UBD (Ubiquitin D), also known as FAT10 (HLA-F adjacent transcript 10), is a ubiquitin-like protein involved in post-translational modification and proteasomal degradation. Discovered in the late 1990s, UBD is encoded near the major histocompatibility complex (MHC) locus on chromosome 6 in humans. It shares structural homology with ubiquitin but functions independently, forming covalent conjugates with target proteins via its C-terminal glycine residue. UBD expression is tightly regulated and primarily induced by pro-inflammatory cytokines, particularly interferon-gamma (IFN-γ) and tumor necrosis factor-alpha (TNF-α), linking it to immune and inflammatory responses.

Antibodies targeting UBD have become essential tools for studying its role in cellular processes, including protein degradation, autophagy, and immune regulation. These antibodies enable detection of UBD in various experimental settings, such as Western blotting, immunohistochemistry, and immunofluorescence. Research using UBD antibodies has revealed its overexpression in certain cancers, autoimmune diseases, and during viral infections, where it may influence antigen presentation by interacting with MHC class I molecules. Additionally, UBD knockout studies suggest its involvement in cell cycle regulation and apoptosis. Despite progress, the full spectrum of UBD's physiological and pathological functions remains under investigation, with antibodies continuing to play a pivotal role in elucidating its complex interactions in health and disease.