Anti-Human C5 Recombinant Antibody (TAB-008) (CAT#: TAB-008)

Chen, Jin Y., et al. "Properdin is a key player in lysis of red blood cells and complement activation on endothelial cells in hemolytic anemias caused by complement dysregulation." Frontiers in immunology 11 (2020): 1460. https://doi.org/10.3389/fimmu.2020.01460

This research investigates the crucial role of properdin in hemolytic anemias caused by complement dysregulation, specifically focusing on paroxysmal nocturnal hemoglobinuria (PNH) and atypical hemolytic uremic syndrome (aHUS). The study developed novel monoclonal antibodies against properdin and established in vitro models using PNH patient red blood cells and human primary endothelial cells. The findings demonstrate that properdin inhibition prevented hemolysis of PNH type II and III red blood cells more effectively than inhibition of Factor B, C3, or C5, with significantly lower molar IC90 values. Additionally, properdin plays a critical role in promoting complement activation on human endothelial cells exposed to heme and rH19-20, conditions that mimic what occurs in aHUS. Inhibition of properdin significantly reduced C3 fragment deposition on endothelial cells, suggesting therapeutic potential for complement-mediated diseases characterized by alternative pathway dysregulation.
Creative Biolabs provided eculizumab, a critical complement inhibitor used as a reference standard throughout the study. This antibody helped establish a comparative benchmark against which the novel anti-properdin monoclonal antibodies could be evaluated. The availability of this well-characterized C5 inhibitor was essential for demonstrating the superior efficacy of properdin inhibition in protecting PNH red blood cells from complement-mediated lysis, particularly in situations where residual hemolysis persists despite eculizumab treatment. This comparison underscored the potential therapeutic value of targeting properdin in complement-mediated hemolytic anemias.