Recombinant Mouse Fc epsilon RI alpha mFc Protein, CF
Recombinant Mouse Fc epsilon RI alpha mFc Protein, CF Summary
- R&D Systems CHO-derived Recombinant Mouse Fc epsilon RI alpha mFc Protein (11646-FC)
- Quality control testing to verify active proteins with lot specific assays by in-house scientists
- All R&D Systems proteins are covered with a 100% guarantee
Product Specifications
| Mouse FCER1a (Ala24-Gln204) Accession # P20489.2 | IEGRMD | Mouse IgG1 (Pro100-Lys330) |
| N-terminus | C-terminus | |
Analysis
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
11646-FC
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. |
| Reconstitution | Reconstitute at 100 μg/mL in water. |
| Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Scientific Data
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Measured by its binding ability in a functional ELISA. Recombinant Mouse Fc epsilon RI alpha mFc Chimera Protein (Catalog # 11646-FC) binds to Human Fc epsilon RI alpha Antibody (AF6678) with an ED50 of 80.0-800 ng/mL.
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2 μg/lane of Recombinant Mouse Fc epsilon RI alpha mFc Chimera Protein (Catalog # 11646-FC) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 67-73 kDa and 130-150 kDa, respectively.
Reconstitution Calculator
Background: Fc epsilon RI alpha
The alpha subunit of the high affinity IgE receptor (Fc epsilon RI alpha or Fc epsilon RIA) is an IgE‑binding type I transmembrane glycoprotein of the multichain immune recognition (MIRR) family (1, 2). The receptor, Fc epsilon RI, is a tetrameric complex of one alpha, one beta and two gamma subunits ( alpha beta gamma 2) on mast cells and basophils (1). An alternate trimeric form ( alpha gamma 2) is expressed on human, but not rodent, mast cells, basophils, eosinophils and professional antigen presenting cells (3). While the gamma subunit is essential for expression of Fc epsilon RI alpha on the cell surface and for cell signaling, the beta subunit, when present, increases the halflife of the Fc epsilon RI complex on the cell surface (3, 4). An isoform of the beta subunit, beta T, blocks processing of the alpha subunit and its cell surface expression (2, 3, 5). Mouse Fc epsilon RI alpha cDNA encodes 250 amino acids (aa) including a 23 aa signal sequence, a 181 aa extracellular domain containing two Ig‑like domains, a 19 aa transmembrane domain and a 27 aa cytoplasmic sequence. Mouse Fc epsilon RI alpha shares 52% and 71% aa sequence identity with human and rat Fc epsilon RI alpha, respectively. Binding of IgE alone increases surface expression of Fc epsilon RI, while crosslinking of IgE/Fc epsilon RI complexes by IgE ligands (allergens) initiates receptor internalization and signaling (2, 4, 5). Mast cell and basophil activation by IgE/Fc epsilon RI crosslinking causes degranulation, releasing histamine, leukotrienes, prostaglandins, and other mediators of immediate‑type and late‑phase allergic reactions. Circulating autoantibodies that crosslink Fc epsilon RI alpha are often found in patients with chronic urticaria (6). Fc epsilon RI on human antigen presenting cells mediates uptake and processing of allergens for presentation by class II MHC (2, 3). Fc epsilon RI expression on human DC and Langerhans cells is up‑regulated during allergic reactions (atopy) and correlates with serum IgE concentration (3).
- Shimizu, A. et al. (1988) Proc. Natl. Acad. Sci. USA 85:1907.
- Abramson, J. and I. Pecht (2007) Immunol. Rev. 217:231.
- Kraft, S. and J-P. Kinet (2007) Nat. Rev. Immunol. 7:365.
- Yamasaki, S. and T. Saito (2008) J. Pharmacol. Sci. 106:336.
- Brenzovich, J. et al. (2009) J. Leukoc. Biol. 86:1351.
- Kikuchi, Y. et al. (2001) J. Allergy Clin. Immunol. 107:1056.
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