FCAR
FCAR (Fc alpha receptor, also known as CD89, FcalphaRI and FcalphaR) is a receptor for the Fc region of IgA. It is a transmembrane glycoprotein of the immunoglobulin superfamily found on myeloid lineage cells, where it mediates immune responses to pathogens. Browse Assay Genie's current range of FCAR research reagents below, or read on for the biology behind the target.
FCAR binds the Fc region of immunoglobulin alpha (IgA). It is a transmembrane glycoprotein present on the surface of myeloid lineage cells such as neutrophils, monocytes, macrophages and eosinophils. When it engages IgA-opsonised targets, it triggers several immune defence processes, including phagocytosis, antibody-dependent cell-mediated cytotoxicity and the release of inflammatory mediators. UniProt also notes that it mediates functions including cytokine production.
The FCAR gene is a member of the immunoglobulin gene superfamily and encodes the immunoglobulin alpha Fc receptor. The protein is found at the cell membrane and also in a secreted form. Multiple alternatively spliced transcript variants encoding different isoforms have been described for this gene, so researchers studying the FCAR protein should consider which isoform is relevant to their work.
HGNC classifies the gene within the CD molecules, immunoglobulin-like domain containing and Fc receptors groups. Its aliases include CD89, FcalphaRI and FcalphaR, and earlier approved names were Fc fragment of IgA, receptor for, and Fc fragment of IgA receptor. Because FCAR links IgA to effector functions in myeloid cells, it is a common subject in studies of antibody-mediated immunity and mucosal defence.
FCAR is present on neutrophils, monocytes, macrophages and eosinophils, making it a useful marker for studying how myeloid cells respond to pathogens.
The receptor links IgA-opsonised targets to phagocytosis and antibody-dependent cell-mediated cytotoxicity, so it is central to work on IgA-mediated immunity.
Receptor engagement stimulates the release of inflammatory mediators and cytokine production, which makes FCAR relevant to studies of inflammatory signalling.
As an immunoglobulin superfamily member and CD molecule, FCAR is studied alongside other Fc receptors to compare antibody isotype recognition.
FCAR binds the Fc region of IgA. On myeloid cells it interacts with IgA-opsonised targets and triggers phagocytosis, antibody-dependent cell-mediated cytotoxicity and the release of inflammatory mediators. UniProt also lists cytokine production among the functions it mediates.
FCAR is also called CD89, FcalphaRI and FcalphaR. Its HGNC name is Fc alpha receptor, and UniProt calls it immunoglobulin alpha Fc receptor. NCBI reports multiple alternatively spliced transcript variants encoding different isoforms, so check which isoform a reagent recognises.
FCAR is a transmembrane glycoprotein on the surface of myeloid lineage cells, including neutrophils, monocytes, macrophages and eosinophils. UniProt lists both cell membrane and secreted locations. Mouse and rat orthologs are not specified in the data here, so check the datasheet of any product for its validated reactivity.
Other Fc receptors, CD molecules and myeloid immune markers with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P24071; product specifications from Assay Genie datasheets.