FCAR抗体

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     Gel: 8%SDS-PAGE, Lysate: 40 μg, Lane: 293T cells, Primary antibody: P08323(FCAR Antibody) at dilution 1/550, Secondary antibody: Goat anti rabbit IgG at 1/8000 dilution, Exposure time: 10 seconds    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human liver cancer tissue using P08323(FCAR Antibody) at dilution 1/20. (Original magnification: ×200)    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human prostate cancer tissue using P08323(FCAR Antibody) at dilution 1/20. (Original magnification: ×200)    

  
  

Fc alpha receptor (FCAR), also known as CD89. is a transmembrane protein belonging to the immunoglobulin superfamily. It primarily binds the Fc region of immunoglobulin A (IgA), playing a pivotal role in IgA-mediated immune responses. Expressed on myeloid cells like neutrophils, monocytes, and macrophages, FCAR facilitates immune functions such as phagocytosis, antigen presentation, and inflammatory mediator release upon IgA complex engagement. Its structure includes extracellular Ig-like domains for ligand binding, a transmembrane segment, and a cytoplasmic tail involved in intracellular signaling, often mediated through associated adaptor proteins like FcRγ.

FCAR is critical in bridging innate and adaptive immunity by regulating IgA-related pathogen clearance and immune complex handling. Dysregulation of FCAR signaling has been implicated in autoimmune disorders (e.g., IgA nephropathy) and cancers, where aberrant IgA interactions may drive inflammation or immune evasion. Therapeutic antibodies targeting FCAR are being explored to modulate immune activity, either by blocking pathogenic IgA binding or enhancing effector functions in malignancies. Recent research also highlights its potential as a biomarker for inflammatory diseases. Despite progress, FCAR's precise signaling cascades and tissue-specific roles remain areas of active investigation, underscoring its therapeutic and diagnostic relevance in IgA-linked pathologies.