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FCAR is a member of the immunoglobulin gene superfamily and encodes a receptor for the Fc region of IgA. Additionally we are shipping Fc Fragment of IgA, Receptor For Antibodies (185) and Fc Fragment of IgA, Receptor For Kits (6) and many more products for this protein.
Showing 10 out of 12 products:
Human FCAR Protein expressed in Human Cells - ABIN2002803
Pasquier, Launay, Kanamaru, Moura, Pfirsch, Ruffié, Hénin, Benhamou, Pretolani, Blank, Monteiro: Identification of FcalphaRI as an inhibitory receptor that controls inflammation: dual role of FcRgamma ITAM. in Immunity 2005
Show all 5 references for ABIN2002803
Rat (Rattus) FCAR Protein expressed in Human Cells - ABIN2009032
Maliszewski, March, Schoenborn, Gimpel, Shen: Expression cloning of a human Fc receptor for IgA. in The Journal of experimental medicine 1991
Show all 5 references for ABIN2009032
have mapped the IgA binding site of bovine IgA Fc receptor and show that, in common with CD89, Tyr-35 in the B-C loop is essential for IgA binding
Findings suggest a basis for the use of Fc receptor I for IgA (FcalphaRI) as a molecular target for the treatment of lupus.
this study examined the expression of IL-4 mRNA, IFN-c mRNA and FcaRI mRNA in tonsillar mononuclear cells of IgA nephropathy9(IgAN) patients and non-IgAN patients.
FCAR polymorphism is not associated with high susceptibility to IGA nephropathy in caucasians.
Abnormally glycosylated IgA1 and soluble CD89-IgA and IgA-IgG complexes, features of primary IgA nephropathy, are also present in alcoholic cirrhosis.
Genetic variation at the promoter region of IgA receptor is associated with IgA nephropathy.
These results suggest a role of anti-FcaRI Fab (show FANCB Proteins) as a negative regulator in controlling the magnitude of the innate immune response
Glycosylation of the CH2 (show Acyp1 Proteins)/CH3 (show SOX3 Proteins) interface inhibits interaction with the pathogen IgA binding protein SSL7, while maintaining binding of pIgR (show PIGR Proteins), essential to the biosynthesis and transport of SIgA.
There is an association between the levels of sCD89-IgA complexes in serum and the severity of IgA nephropathy, and a possible genetic component in regulating the production or expression of sCD89.
Endocytosis of FcalphaR is clathrin- and dynamin (show DNM1 Proteins)-dependent, but is not regulated by Rab5 (show RAB5A Proteins), and the endocytic motif is not located in the cytoplasmic domain of FcalphaR.
CD89 circulates in a high molecular mass form in complex covalently linked to IgA and contributes to the formation of polymeric serum IgA.
This gene is a member of the immunoglobulin gene superfamily and encodes a receptor for the Fc region of IgA. The receptor is a transmembrane glycoprotein present on the surface of myeloid lineage cells such as neutrophils, monocytes, macrophages, and eosinophils, where it mediates immunologic responses to pathogens. It interacts with IgA-opsonized targets and triggers several immunologic defense processes, including phagocytosis, antibody-dependent cell-mediated cytotoxicity, and stimulation of the release of inflammatory mediators. Multiple alternatively spliced transcript variants encoding different isoforms have been described for this gene.
IgA Fc receptor
, immunoglobulin A Fc receptor
, immunoglobulin alpha Fc receptor
, Fc fragment of IgA, receptor for, isoform 7
, Fc alpha receptor