USP3抗体—艾普蒂

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     The image is immunohistochemistry of paraffin-embedded Human thyroid cancer tissue using P09329(USP3 Antibody) at dilution 1/30. (Original magnification: ×200)    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human gastric cancer tissue using P09329(USP3 Antibody) at dilution 1/30. (Original magnification: ×200)    

  
  

The USP3 antibody targets ubiquitin-specific protease 3 (USP3), a deubiquitinating enzyme (DUB) belonging to the ubiquitin-specific protease family. USP3 plays a critical role in maintaining genomic stability by regulating DNA repair, chromatin remodeling, and cell cycle progression. It catalyzes the removal of ubiquitin chains from substrates, counteracting ubiquitin-mediated signaling. Research highlights its involvement in modulating key pathways, including the DNA damage response (DDR) via interactions with proteins like γH2AX and RAD51. as well as regulating NF-κB signaling by deubiquitinating TRAF proteins. USP3 is also implicated in cancer, where its dysregulation may influence tumor progression, metastasis, and chemoresistance.

Antibodies against USP3 are widely used in research to study its expression, localization, and molecular functions. They enable techniques like Western blotting, immunofluorescence, and co-immunoprecipitation to explore USP3’s role in cellular processes and disease contexts. Studies using USP3 antibodies have revealed its nuclear localization and overexpression in certain cancers, suggesting its potential as a therapeutic target. Recent work also links USP3 to viral infection responses and immune regulation. However, challenges remain in fully characterizing its substrate specificity and context-dependent roles. Commercially available USP3 antibodies vary in specificity, requiring validation via knockout controls to ensure reliability in experimental settings.