TDP43抗体—艾普蒂

+ +

•  

   

     Black line: Control Antigen (100 ng);Purple line: Antigen (10ng); Blue line: Antigen (50 ng); Red line:Antigen (100 ng)    

  
  

•  

   

     Western blot analysis using TDP43 mouse mAb against Hela (1), HEK293 (2), MCF-7 (3), and A549 (4) cell lysate.    

  
  

•  

   

     Immunofluorescence analysis of Hela cells using TDP43 mouse mAb (green). Blue: DRAQ5 fluorescent DNA dye. Red: Actin filaments have been labeled with Alexa Fluor- 555 phalloidin. Secondary antibody from Fisher (Cat#: 35503)    

  
  

•  

   

     Flow cytometric analysis of A431 cells using TDP43 mouse mAb (green) and negative control (red).    

  
  

•  

   

     Flow cytometric analysis of Hela cells using TDP43 mouse mAb (green) and negative control (red).    

  
  

•  

   

     Flow cytometric analysis of HepG2 cells using TDP43 mouse mAb (green) and negative control (red).    

  
  

•  

   

     Immunohistochemical analysis of paraffin-embedded human baldder cancer tissues using TDP43 mouse mAb with DAB staining.    

  
  

•  

   

     Immunohistochemical analysis of paraffin-embedded human liver cancer tissues using TDP43 mouse mAb with DAB staining.    

  
  

•  

   

     Immunohistochemical analysis of paraffin-embedded human rectal cancer tissues using TDP43 mouse mAb with DAB staining.    

  
  

TAR DNA-binding protein 43 (TDP-43) is a ubiquitously expressed RNA-binding protein encoded by the *TARDBP* gene. It plays critical roles in RNA metabolism, including splicing, transport, and stability. Pathologically, TDP-43 is a major component of aberrant protein aggregates observed in neurodegenerative diseases such as amyotrophic lateral sclerosis (ALS), frontotemporal lobar degeneration (FTLD-TDP), and Alzheimer’s disease. In these conditions, TDP-43 undergoes mislocalization from the nucleus to the cytoplasm, forming hyperphosphorylated, ubiquitinated inclusions that disrupt cellular function and contribute to neurodegeneration.

Antibodies targeting TDP-43 are essential tools for studying its physiological and pathological roles. They enable detection of both normal nuclear TDP-43 and pathological aggregates in tissues or cell models using techniques like immunohistochemistry, Western blotting, or immunofluorescence. Specific antibodies can distinguish between normal and disease-associated forms (e.g., phosphorylated or truncated TDP-43), aiding in disease diagnosis and mechanistic research. Additionally, TDP-43 antibodies are used to explore its interactions with RNA or other proteins, its role in stress granule dynamics, and the effects of *TARDBP* mutations linked to familial ALS.

Challenges include ensuring antibody specificity due to post-translational modifications or structural changes in pathological TDP-43. Despite this, these antibodies remain vital for advancing understanding of TDP-43 proteinopathies and developing targeted therapies.