| Reactivity | HuSpecies Glossary |
| Applications | Bioactivity |
| Format | Carrier-Free |
| Additional Information | Biotinylated Avi-tag His-tag |
| Details of Functionality | Measured by its binding ability in a functional ELISA.<br />When Human IgE is immobilized at 1.00 µg/mL (100 µL/well), Biotinylated Recombinant Human Fc epsilon RI alpha Avi-tag His-tag binds with an ED<sub>50</sub> of 0.300-1.80 ng/mL.<br /><br /> |
| Accession # | |
| N-terminal Sequence | Val26 |
| Structure / Form | Biotinylated via Avi-tag |
| Protein/Peptide Type | Recombinant Proteins |
| Endotoxin Note | <0.100 EU per 1 µg of the protein by the LAL method. |
| Dilutions |
|
| Theoretical MW | 25 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 | 50-60 kDa, under reducing conditions. |
| Storage | Store the unopened product at -20 to -70 °C. Use a manual defrost freezer and avoid repeated freeze-thaw cycles. Do not use past expiration date. |
| Buffer | Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. |
| Reconstitution Instructions | Reconstitute at 500 μg/mL in PBS. |
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). Our Avi-tag Biotinylated Human Fc epsilon RI alpha protein features biotinylation at a single site contained within the Avi-tag, a unique 15 amino acid peptide. Protein orientation will be uniform when bound to streptavidin-coated surface due to the precise control of biotinylation and the rest of the protein is unchanged so there is no interference in the protein's bioactivity.
The concentration calculator allows you to quickly calculate the volume, mass or concentration of your vial. Simply enter your mass, volume, or concentration values for your reagent and the calculator will determine the rest.
| Uniprot |
|
