CD89抗体—艾普蒂

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     Western blot analysis of Caspase7 in C6, 3T3 lysates using Caspase 7 antibody.    

  
  

CD89. also known as FcαRI (Fc alpha receptor I), is a transmembrane glycoprotein primarily expressed on myeloid cells such as neutrophils, monocytes, and macrophages. Discovered in the 1980s, it belongs to the immunoglobulin superfamily and binds the Fc region of immunoglobulin A (IgA), playing a pivotal role in mucosal immunity and inflammatory responses. Structurally, CD89 contains two extracellular immunoglobulin-like domains that mediate IgA interaction, and its cytoplasmic tail triggers intracellular signaling upon ligand engagement.

CD89 bridges innate and adaptive immunity by facilitating IgA-mediated effector functions, including phagocytosis, antibody-dependent cellular cytotoxicity (ADCC), and cytokine release. However, its dual role in immune regulation is notable: while CD89-IgA complexes can neutralize pathogens, excessive activation may contribute to inflammatory diseases like IgA nephropathy or rheumatoid arthritis. Dysregulated CD89 signaling has also been linked to autoimmune disorders and certain cancers.

Therapeutic interest in CD89 antibodies arises from their potential to modulate immune responses. Blocking CD89-IgA interactions could mitigate inflammation in autoimmune conditions, while CD89-targeting bispecific antibodies or antibody-drug conjugates (ADCs) are being explored for cancer therapy. Recent studies focus on optimizing CD89 antibody specificity and minimizing off-target effects. Despite challenges, CD89 remains a promising target for treating IgA-mediated pathologies and enhancing immunotherapy strategies.