USP21抗体—艾普蒂

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     The image is immunohistochemistry of paraffin-embedded Human colorectal cancer tissue using P09325(USP21 Antibody) at dilution 1/35. (Original magnification: ×200)    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human tonsil tissue using P09325(USP21 Antibody) at dilution 1/35. (Original magnification: ×200)    

  
  

USP21 (Ubiquitin-Specific Protease 21) is a deubiquitinating enzyme (DUB) belonging to the ubiquitin-specific protease family, which regulates protein stability and function by removing ubiquitin chains from target substrates. It plays critical roles in diverse cellular processes, including cell cycle progression, signal transduction, and immune response regulation. USP21 is known to deubiquitinate substrates such as histone H2B (influencing chromatin remodeling and gene expression), RIG-I (modulating antiviral innate immunity), and TRAF3 (affecting NF-κB signaling). Dysregulation of USP21 has been implicated in cancers, inflammatory diseases, and neurodegenerative disorders, highlighting its therapeutic potential.

USP21 antibodies are essential tools for studying its expression, localization, and interaction networks. They are widely used in techniques like Western blotting, immunofluorescence, immunoprecipitation, and immunohistochemistry to investigate USP21's biological functions. Researchers often validate these antibodies using USP21-knockout cell lines to ensure specificity. Commercially available USP21 antibodies are typically raised in rabbits or mice, targeting specific epitopes within the protein's conserved regions. Their applications span basic research—such as elucidating USP21's role in Wnt/β-catenin or TNFα/NF-κB pathways—and clinical studies exploring its correlation with tumor progression or drug resistance. Reliable USP21 antibodies are crucial for advancing both mechanistic understanding and therapeutic targeting of USP21-related diseases.