The FCAR antibody binds to CD89, a 50–100 kDa type I transmembrane receptor encoded by the FCAR gene on chromosome 19 . CD89 is part of the multichain immune recognition receptor (MIRR) family and plays a dual role in pro- and anti-inflammatory signaling depending on IgA binding state . The antibody specifically recognizes the extracellular domain of CD89, enabling its use in studying IgA-mediated immune responses .
CD89 contains:
Extracellular domain (ECD): Two C2-type Ig-like domains (EC1 and EC2) oriented at right angles
Transmembrane (TM) domain: 19 amino acids, interacting with the FcR γ-chain for signaling
Cytoplasmic domain: 41 amino acids, facilitating downstream signaling via ITAM motifs
Inside-out signaling: Priming via intracellular signals enables CD89 to bind IgA
Outside-in signaling: Ligand binding triggers inflammatory or anti-inflammatory responses, depending on IgA type (monomeric vs. polymeric)
FcR γ-chain dependency: Required for transport to late endosomes and sustained inflammatory signaling
Research: Investigating IgA-mediated immune responses in mucosal immunity and autoimmune diseases
Therapeutic potential: Engineering FCAR antibodies to modulate IgA signaling for conditions like cancer or inflammatory disorders
Species-specificity: Lack of a murine ortholog limits in vivo studies
Therapeutic optimization: Balancing anti-inflammatory and pro-inflammatory signals remains critical
Glycosylation variability: Impact of post-translational modifications on FCAR function is under investigation