Human IgG1抗体;Human IgG1 Antibody—艾普蒂 新品

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     Western blot analysis of Thrombomodulin / CD141 expression in mouse lung cell lysate.    

  
  

Human IgG1 is the most abundant immunoglobulin subclass in human serum, playing a central role in adaptive immunity. As a Y-shaped glycoprotein, it consists of two identical heavy chains and two light chains linked by disulfide bonds. Its structure includes two antigen-binding Fab regions that recognize specific pathogens and a conserved Fc region that interacts with immune cells. IgG1 excels in effector functions: it neutralizes pathogens, activates the complement cascade via the classical pathway, and triggers antibody-dependent cellular cytotoxicity (ADCC) or phagocytosis (ADCP) by binding Fcγ receptors on immune cells.

Notably, IgG1 has a long serum half-life (~21 days) due to pH-dependent recycling mediated by the neonatal Fc receptor (FcRn). This stability, combined with robust effector activity, makes it a preferred backbone for therapeutic monoclonal antibodies. Drugs like rituximab, trastuzumab, and immune checkpoint inhibitors leverage IgG1’s Fc domain to enhance clinical efficacy. However, engineered modifications to its Fc region (e.g., amino acid substitutions or glycosylation changes) are often employed to fine-tune immune activation or reduce side effects.

Balancing target engagement and immune modulation, IgG1 remains pivotal in treating cancers, autoimmune diseases, and infections, reflecting its versatile biological and therapeutic profile.