SPDL1抗体

+ +

•  

   

     Gel: 8%SDS-PAGE, Lysate: 40 μg, Lane 1-6: Hela, 293T, Jurkat cell, Mouse testis tissue, K562, A549 cell lysates , Primary antibody: P00709(SPDL1 Antibody) at dilution 1/700, Secondary antibody: Goat anti rabbit IgG at 1/5000 dilution, Exposure time: 1 minute    

  
  

•  

   

     The image is immunohistochemistry of paraffin-embedded Human thyroid cancer tissue using P00709(SPDL1 Antibody) at dilution 1/100. (Original magnification: ×200)    

  
  

•  

   

     The image is immunohistochemistry of paraffin-embedded Human prostate cancer tissue using P00709(SPDL1 Antibody) at dilution 1/100. (Original magnification: ×200)    

  
  

SPDL1 (Spindle Apparatus Coiled-Coil Domain Protein 1), also known as CCDC99. is a critical component of the spindle assembly checkpoint (SAC), a surveillance mechanism ensuring accurate chromosome segregation during mitosis. It localizes to the spindle midzone and plays a role in maintaining genomic stability by regulating the timing of anaphase onset. SPDL1 interacts with key SAC proteins, including MAD2 and the dynein motor complex, facilitating the removal of checkpoint signals from kinetochores once chromosomes achieve proper attachment. Dysregulation of SPDL1 is linked to mitotic errors, chromosomal instability, and carcinogenesis, making it a potential biomarker or therapeutic target in cancers.

SPDL1 antibodies are essential tools for studying its expression, localization, and function in cell cycle regulation. These antibodies are widely used in techniques like Western blotting, immunofluorescence, and immunohistochemistry to investigate SPDL1’s role in mitotic progression, SAC signaling, and its association with tumorigenesis. Recent studies explore SPDL1’s overexpression in certain cancers (e.g., hepatocellular carcinoma) and its correlation with poor prognosis. Additionally, SPDL1 antibodies aid in deciphering molecular mechanisms underlying resistance to anti-mitotic drugs, offering insights for developing novel cancer therapies targeting mitotic fidelity. Their specificity and reliability remain crucial for advancing research in cell biology and oncology.