UBA7抗体—艾普蒂

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     The image is immunohistochemistry of paraffin-embedded Human liver cancer tissue using P08932(UBA7 Antibody) at dilution 1/110. (Original magnification: ×200)    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human colorectal cancer tissue using P08932(UBA7 Antibody) at dilution 1/110. (Original magnification: ×200)    

  
  

UBA7 (Ubiquitin-like modifier-activating enzyme 7), also known as UBE2L7. is a member of the E2 ubiquitin-conjugating enzyme family. It plays a critical role in the ubiquitin-proteasome system (UPS), which regulates protein degradation and cellular homeostasis. Specifically, UBA7 is essential for activating and transferring ubiquitin-like protein ISG15 (interferon-stimulated gene 15) to target proteins, a process vital for antiviral immune responses and inflammatory regulation. This enzyme is induced by type I interferons, linking it to innate immunity and host defense mechanisms against viral infections.

UBA7 antibodies are crucial tools for studying its expression, localization, and function in various biological contexts. They are widely used in techniques like Western blotting, immunoprecipitation, and immunofluorescence to investigate UBA7’s role in diseases such as cancer, autoimmune disorders, and neurodegenerative conditions. Dysregulation of UBA7 has been implicated in tumorigenesis due to its impact on protein stability and signaling pathways. Additionally, research highlights its interaction with viral proteins, suggesting therapeutic targeting potential.

Commercial UBA7 antibodies are typically validated for specificity using knockout cell lines or siRNA knockdown. Researchers prioritize antibodies with high affinity and minimal cross-reactivity to related E2 enzymes. Understanding UBA7’s molecular mechanisms through these antibodies advances insights into UPS-related pathologies and therapeutic strategies.