CDC34抗体;CDC34 Antibody—艾普蒂

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     Gel: 12%SDS-PAGE, Lysate: 40 μg, Lane: Human left the thymus tissue lysate, Primary antibody: P12717(CDC34 Antibody) at dilution 1/200, Secondary antibody: Goat anti rabbit IgG at 1/8000 dilution, Exposure time: 2 minutes    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human tonsil tissue using P12717(CDC34 Antibody) at dilution 1/20. (Original magnification: ×200)    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human colorectal cancer tissue using P12717(CDC34 Antibody) at dilution 1/20. (Original magnification: ×200)    

  
  

The CDC34 antibody is a crucial tool in studying the CDC34 protein, a member of the E2 ubiquitin-conjugating enzyme family encoded by the *UBE2R1* gene in humans. CDC34 plays a pivotal role in the ubiquitin-proteasome system, primarily by collaborating with SCF (Skp1-Cullin-F-box) E3 ligase complexes to regulate protein degradation. This enzyme is essential for cell cycle progression, particularly during the G1-to-S phase transition, where it targets inhibitors like p27^Kip1 and p21^Cip1 for proteasomal degradation. Dysregulation of CDC34 is implicated in cancer, neurodegenerative diseases, and immune disorders due to its role in maintaining protein homeostasis and signaling pathways.

CDC34 antibodies are widely used in research to detect protein expression, localization, and post-translational modifications via techniques such as Western blotting, immunohistochemistry (IHC), and immunoprecipitation (IP). These antibodies help elucidate CDC34’s interaction networks, substrate specificity, and regulatory mechanisms. For example, studies using CDC34-specific antibodies have revealed its overexpression in certain cancers, linking it to tumor proliferation and chemoresistance. Additionally, they aid in exploring CDC34’s involvement in DNA repair and apoptosis.

As therapeutic targeting of ubiquitination pathways gains momentum, CDC34 antibodies also serve as vital reagents for drug discovery, enabling validation of inhibitors aimed at modulating SCF ligase activity. However, challenges remain in ensuring antibody specificity due to structural similarities among E2 enzymes. Ongoing research continues to refine these tools, enhancing their utility in both basic and translational studies.