+ +

•  

   

     Western blot analysis of Cdc23/APC8 expression in (1)HepG2 cell lysate; (2)Jurkat cell lysate.    

  
  

•  

   

     All lanes use the Antibody at 1:2K dilution for 1 hour at room temperature.    

  
  

•  

   

     All lanes use the Antibody at 1:2K dilution for 1 hour at room temperature.    

  
  

•  

   

     Immunofluorescent analysis using the Antibody at 1:50 dilution.    

  
  

•  

   

     Immunofluorescent analysis using the Antibody at 1:50 dilution.    

  
  

The Cdc23/APC8 antibody targets a conserved subunit of the Anaphase-Promoting Complex/Cyclosome (APC/C), a multi-subunit E3 ubiquitin ligase critical for cell cycle regulation. In yeast, Cdc23 (Cell Division Cycle 23) corresponds to the human APC8 (also known as CDC23), which is part of the APC/C core essential for substrate recognition and complex assembly. The APC/C orchestrates the ubiquitination of key cell cycle regulators, such as cyclins and securins, marking them for proteasomal degradation. This process ensures timely progression through mitosis, exit from mitosis, and maintenance of the G1 phase.

The Cdc23/APC8 subunit plays a structural role in stabilizing the APC/C architecture and facilitating interactions with co-activators like Cdc20 or Cdh1. Antibodies against Cdc23/APC8 are widely used to study APC/C composition, dynamics, and function in various experimental models. They enable detection of APC/C levels in immunoblotting, immunoprecipitation assays, or localization studies during cell cycle phases. Dysregulation of APC/C activity is linked to genomic instability and cancer, making these antibodies valuable tools for investigating mitotic errors, checkpoint mechanisms, and oncogenic pathways. Researchers also utilize them to explore developmental defects or therapeutic targets tied to APC/C dysfunction. Specificity validation, including knockout controls, is recommended due to the complex’s multi-protein nature.