CUL3抗体

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     Gel: 6%SDS-PAGE, Lysate: 40 μg, Lane: 293T cells, Primary antibody: P00300(CUL3 Antibody) at dilution 1/250, Secondary antibody: Goat anti rabbit IgG at 1/8000 dilution, Exposure time: 20 seconds    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human thyroid cancer tissue using P00300(CUL3 Antibody) at dilution 1/30. (Original magnification: ×200)    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human colon cancer tissue using P00300(CUL3 Antibody) at dilution 1/30. (Original magnification: ×200)    

  
  

CUL3 (Cullin 3) is a core component of the Cullin-RING ligases (CRLs), a family of multi-subunit E3 ubiquitin ligase complexes that mediate protein ubiquitination and degradation via the proteasome. As a scaffold protein, CUL3 binds to RING proteins (e.g., RBX1) and substrate-specific adaptors (e.g., BTB-domain proteins), enabling the targeted polyubiquitination of proteins involved in diverse cellular processes, including cell cycle regulation, stress responses, and signal transduction. CUL3 antibodies are essential tools for studying its expression, localization, and interactions in these pathways.

Dysregulation of CUL3 is linked to diseases such as cancer, hypertension, and neurological disorders. For example, mutations in CUL3 or its adaptors (e.g., KEAP1 in the KEAP1-CUL3 complex) disrupt NRF2 degradation, leading to oxidative stress resistance in tumors. In hypertension, CUL3 variants impair vascular tone regulation. CUL3 antibodies are widely used in techniques like Western blotting, immunofluorescence, and co-immunoprecipitation to investigate these mechanisms.

Research also highlights CUL3's role in developmental processes and autophagy. Its involvement in ubiquitinating specific substrates, such as cyclin E or Rho GTPases, underscores its importance in maintaining cellular homeostasis. Commercial CUL3 antibodies are validated for species reactivity (human, mouse, rat) and application-specific efficacy, aiding both basic research and clinical studies targeting ubiquitination pathways.