Recombinant Human Fc epsilon RI alpha His-tag Protein, CF New
Recombinant Human Fc epsilon RI alpha His-tag Protein, CF Summary
Product Specifications
Val26-Gln205, with a C-terminal 6-His tag
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.
11536-FC
Formulation | Supplied as a 0.2 μm filtered solution in PBS with Trehalose. |
Shipping | The product is shipped with dry ice or equivalent. 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
Measured by its binding ability in a functional ELISA. Recombinant Human Fc epsilon RI alpha His-tag Protein binds to human IgE with an ED50 of less than 100 ng/mL.
2 μg/lane of Recombinant Human Fc epsilon RI alpha His-tag Protein (Catalog # 11536-FC) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 48-55 kDa, under reducing conditions.
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). Human Fc epsilon RI alpha cDNA encodes 257 amino acids (aa) including a 25 aa signal sequence, a 180 aa extracellular domain containing two Ig‑like domains that bind IgE and an endoplasmic reticulum retention motif, a 21 aa transmembrane domain with a charged amino acid (Asp219) that contributes to intracellular transport, and a 32 aa cytoplasmic sequence (1, 3, 6). Human Fc epsilon RI alpha shares 50-62% aa sequence identity with mouse, rat, equine, ovine, bovine, porcine and canine Fc epsilon RI alpha. 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 (7). 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.
- Cauvi, D.M. et al. (2006) J. Biol. Chem. 281:10448.
- Kikuchi, Y. et al. (2001) J. Allergy Clin. Immunol. 107:1056.
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