FADD抗体—艾普蒂

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

  
  

FADD (Fas-associated protein with death domain) is a pivotal adaptor protein involved in programmed cell death (apoptosis) and inflammatory signaling. Structurally, it contains a C-terminal death domain (DD) that mediates interactions with death receptors like Fas (CD95), TRAIL receptors, and TNFR1. as well as an N-terminal death effector domain (DED) responsible for recruiting initiator caspases (e.g., caspase-8/10). Upon receptor activation, FADD oligomerizes to form the death-inducing signaling complex (DISC), triggering caspase activation and apoptosis. Beyond apoptosis, FADD participates in non-apoptotic processes, including cell cycle regulation, proliferation, autophagy, and necroptosis, through interactions with other signaling molecules like RIPK1 and TRADD.

FADD dysregulation is implicated in cancer, autoimmune disorders, and neurodegenerative diseases. For instance, reduced FADD expression may promote tumor survival, while excessive FADD activity can drive inflammatory pathologies. FADD-specific antibodies are essential tools for studying its expression, localization, and interactions in these contexts. They are widely used in techniques such as Western blotting, immunohistochemistry, and co-immunoprecipitation to elucidate FADD's role in health and disease. Research utilizing FADD antibodies continues to advance understanding of cell death mechanisms and therapeutic strategies targeting apoptosis-related pathways.