ECD抗体

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

  
  

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     Western blot analysis using UCHL1 mouse mAb against mouse brain (1), and rat brain (2) cell lysate.    

  
  

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     Immunofluorescence analysis of Hela cells using UCHL1 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)    

  
  

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     Flow cytometric analysis of Hek293 cells using UCHL1 mouse mAb (green) and negative control (red).    

  
  

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     Immunohistochemical analysis of paraffin-embedded human ovarian cancer tissues using UCHL1 mouse mAb with DAB staining.    

  
  

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     Immunohistochemical analysis of paraffin-embedded human brain tissues using UCHL1 mouse mAb with DAB staining.    

  
  

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     Immunohistochemical analysis of paraffin-embedded human endometrial cancer tissues using UCHL1 mouse mAb with DAB staining.    

  
  

ECD antibodies target the extracellular domain (ECD) of transmembrane proteins, which are critical components in cell signaling, adhesion, and receptor-ligand interactions. These antibodies are widely used in biomedical research and therapeutic development due to their ability to bind surface-exposed regions of proteins like receptor tyrosine kinases, cytokine receptors, or cell adhesion molecules. By blocking or modulating ECD-mediated functions, they help study protein activity, cellular communication, and disease mechanisms.

In therapeutics, ECD-specific antibodies are foundational for monoclonal antibody (mAb) drugs, such as trastuzumab (targeting HER2/neu in breast cancer) or cetuximab (anti-EGFR for colorectal cancer). They inhibit ligand binding, receptor dimerization, or downstream signaling, offering precision in cancer and autoimmune disease treatments. Diagnostic applications include biomarker detection in ELISA, flow cytometry, or immunohistochemistry, aiding disease diagnosis and monitoring.

ECD antibodies are typically generated using recombinant ECD fragments as immunogens. Their specificity depends on conformational epitopes, requiring careful validation to avoid cross-reactivity. Challenges include preserving native protein folding during antigen production and ensuring functional affinity. Advances in structural biology and phage display libraries have improved ECD antibody development, enhancing their utility in both research and clinical settings.