Recombinant Human FCAR/CD89 Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Binding Activity
Format
Carrier-Free

Order Details

Recombinant Human FCAR/CD89 Protein, CF Summary

Details of Functionality
Measured by its ability to bind human lgA in a functional ELISA with an estimated
KD <10 nM.
Source
Mouse myeloma cell line, NS0-derived human FCAR/CD89 protein
Gln22-Asn227, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
No results obtained: Gln22 predicted
Protein/Peptide Type
Recombinant Proteins
Gene
FCAR
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Theoretical MW
24.3 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
40-50 kDa, reducing conditions
Publications
Read Publications using
3939-FA in the following applications:

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human FCAR/CD89 Protein, CF

  • CD89 antigen
  • CD89
  • CD89IgA Fc receptor
  • Fc alpha receptor
  • Fc fragment of IgA, receptor for
  • FCAR
  • immunoglobulin alpha Fc receptor

Background

FCAR, also called Fc alpha RI or CD89, is a variably glycosylated 50-100 kDa myeloid-specific type I transmembrane (TM) Fc receptor for IgA that is a member of the multichain immune recognition receptor (MIRR) family (1-3). Human FCAR contains a 21 amino acid (aa) signal sequence and extracellular (ECD), TM and cytoplasmic domains of 206, 19 and 41 aa, respectively (4). Arg230 within the TM domain supports interaction with the ITAM-containing signaling subunit, FcR gamma, which contains a TM Asp (5-7). Two ECD C2-type Ig-like domains (EC1 and 2) are oriented at right angles (8). Up to two molecules of FCAR can bind one molecule of serum IgA via EC1 (8). Many splice variants have been reported, but only two have been identified as proteins (9, 10). The a.2 form, which lacks 22 aa just prior to the TM domain, is exclusively expressed in alveolar macrophages. The a.3 form lacks EC2. FCAR binds monomeric, polymeric and secretory IgA, but does not mediate the barrier function of secretory IgA in mucosal epithelium (1-3). Shedding and circulation of polymeric IgA/FCAR immune complexes has been reported (11). Circulating neutrophils, eosinophils, and monocytes express FCAR (12). Tissue expression of FCAR is mainly from neutrophils; FCAR is downregulated as monocytes differentiate to tissue macrophages (12). On neutrophils, a significant amount of FCAR lacks FcR gamma, but can still be endocytosed to early endosomes and recycled to the cell surface (5). Binding of serum IgA to FCAR is transient and anti-inflammatory, inhibiting IgG or IgE-induced degranulation (6). Sustained aggregation of FCAR results in inflammatory responses (6). FcR gamma signaling is required for these and for transport to late endosomes (5-7). Human FCAR shows 55-58% aa identity with rat, horse and cow FCAR. No ortholog occurs in mouse. FCAR structure resembles the KIR/ILT/LIR/MIR family more than other IgA receptors, including pIgR, Fc alpha /μR, asialoglycoprotein receptor (ASGR1) and transferrin receptor (TfR) (1-3).
  1. Wines, B. D. and P. M. Hogarth (2006) Tissue Antigens 68:103.
  2. Otten, M. A. and M. van Egmon (2004) Immunol. Lett. 92:23.
  3. Montiero, R. C. and J. G. J. van de Winkel (2003) Annu. Rev. Immunol. 21:177.
  4. Maliszewski, C. R. et al. (1990) J. Exp. Med. 172:1665.
  5. Launay, P. et al. (1999) J. Biol. Chem. 274:7216.
  6. Pasquier, B. et al. (2005) Immunity 22:31.
  7. Shen, L. et al. (2001) Blood 97:205.
  8. Herr, Y. et al. (2003) Nature 423:614.
  9. Patry, C. et al. (1996) J. Immunol. 156:4442.
  10. Togo, S. et al. (2003) FEBS Lett. 535:205.
  11. van der Boog, P. J. M. et al. (2002) J. Immunol. 168:1252.
  12. Hamre, R. et al. (2003) Scand. J. Immunol. 57:506.

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Publications for FCAR/CD89 (3939-FA)(2)

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Bioinformatics

Gene Symbol FCAR
Uniprot