FCAR Human
Sf9, Baculovirus cells.
Fc Fragment Of IgA Receptor, Fc Fragment Of IgA, Receptor For, CD89, Immunoglobulin Alpha Fc Receptor, Fc Alpha Receptor, FCAR Variant 14, IgA Fc Receptor, CD89 Antigen, CTB-61M7.2, FcalphaRI, Immunoglobulin alpha Fc receptor, IgA Fc receptor.
Greater than 85.0% as determined by SDS-PAGE.
Description
FCAR produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 215 amino acids (22-227a.a.) and having a molecular mass of 24.5kDa. (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).
FCAR is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Product Specs
The Fc Fragment Of IgA Receptor, also known as FCAR, is a member of the multichain immune recognition receptor family. IgA, the antibody that binds to FCAR, is the most abundant immunoglobulin in mucosal areas, though it is the second most common antibody isotype in serum. FCAR plays a role in both pro-inflammatory and anti-inflammatory responses depending on the state of the IgA that is bound to it. FCAR is also a key Fc receptor for the neutrophil-mediated killing of tumor cells. When neutrophils expressing FCAR interact with tumor cells that have been opsonized with IgA, the neutrophils exhibit antibody-dependent cell-mediated cytotoxicity and release the cytokines TNF-α and IL-1β, which lead to increased neutrophil migration to the tumor site.
Produced in Sf9 Baculovirus cells, FCAR is a single, glycosylated polypeptide chain with a molecular weight of 24.5 kDa. It consists of 215 amino acids (22-227a.a.). On SDS-PAGE, the molecular size will appear to be approximately 28-40 kDa. FCAR is expressed with a 9 amino acid His tag at the C-terminus and purified using proprietary chromatographic techniques.
The FCAR protein solution (0.25 mg/mL) is supplied in Phosphate Buffered Saline (pH 7.4) with 10% glycerol.
For short-term storage (2-4 weeks), store at 4°C. For extended storage, freeze at -20°C. Adding a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Avoid repeated freeze-thaw cycles.
Purity is determined to be greater than 85.0% by SDS-PAGE analysis.
Fc Fragment Of IgA Receptor, Fc Fragment Of IgA, Receptor For, CD89, Immunoglobulin Alpha Fc Receptor, Fc Alpha Receptor, FCAR Variant 14, IgA Fc Receptor, CD89 Antigen, CTB-61M7.2, FcalphaRI, Immunoglobulin alpha Fc receptor, IgA Fc receptor.
Sf9, Baculovirus cells.
ADPQEGDFPM PFISAKSSPV IPLDGSVKIQ CQAIREAYLT QLMIIKNSTY REIGRRLKFW NETDPEFVID HMDANKAGRY QCQYRIGHYR FRYSDTLELV VTGLYGKPFL SADRGLVLMP GENISLTCSS AHIPFDRFSL AKEGELSLPQ HQSGEHPANF SLGPVDLNVS GIYRCYGWYN RSPYLWSFPS NALELVVTDS IHQDYTTQNH HHHHH.
Product Science Overview
The Fc fragment of IgA receptor, also known as FcαRI or CD89, is a type I transmembrane receptor that plays a crucial role in the immune system. It is primarily expressed on myeloid cells such as neutrophils, eosinophils, monocytes, subsets of dendritic cells, and macrophages . The receptor is responsible for binding the Fc region of Immunoglobulin A (IgA), which is the most abundantly produced antibody isotype in humans .
The FcαRI receptor is composed of two extracellular immunoglobulin-like domains, a transmembrane domain, and a cytoplasmic tail . The Fc region of IgA, which binds to FcαRI, is derived from the second and third constant domains of the antibody’s heavy chains . This interaction is essential for the receptor-mediated activity of IgA, including its role in immune responses and inflammation .
FcαRI plays a dual role in the immune system. On one hand, it can mediate inhibitory signals that suppress immune responses, thereby preventing the development of autoimmunity and inflammation . On the other hand, when IgA is aggregated, it can induce sustained activation through FcαRI, leading to inflammatory diseases . This Janus-like nature of FcαRI is due to the heterogeneity in molecular forms of IgA and their interaction with the receptor .
The Fc fragment of IgA receptor has significant therapeutic potential. FcαRI-mediated inhibitory functions have been shown to suppress several inflammatory diseases in animal models, including asthma and glomerulonephritis . Intravenous monomeric IgA (mIgAIV) and anti-FcαR monovalent antibodies are being explored as promising tools for immunotherapy .
