Recombinant Mouse High affinity immunoglobulin epsilon receptor subunit alpha (Fcer1a) is produced using an in vitro E.coli expression system, spanning the full mature protein length from amino acids 24 to 250. This protein carries an N-terminal 10xHis-SUMO tag, which provides easier purification and enhanced stability. The product achieves over 90% purity as confirmed by SDS-PAGE, making it appropriate for various research applications.
The High affinity immunoglobulin epsilon receptor subunit alpha (Fcer1a) appears to be a crucial component of the immunoglobulin E (IgE) receptor complex, largely involved in allergic responses. It likely plays a central role in the signal transduction pathway that triggers mediator release from mast cells and basophils. Understanding Fcer1a may be essential for research into allergy mechanisms and developing therapeutic interventions.
Potential Applications
Note: The applications listed below are based on what we know about this protein's biological functions, published research, and experience from experts in the field. However, we haven't fully tested all of these applications ourselves yet. We'd recommend running some preliminary tests first to make sure they work for your specific research goals.
1. Antibody Development and Validation Studies
This recombinant mouse Fcer1a protein can function as an immunogen or coating antigen for developing monoclonal or polyclonal antibodies specific to the high affinity IgE receptor alpha subunit. The N-terminal His-SUMO tag enables purification and immobilization on different surfaces for ELISA-based antibody screening and characterization. Researchers might use this protein to validate antibody specificity through Western blot, immunoprecipitation, and competitive binding assays. The high purity (>90%) appears to ensure reliable and reproducible results in antibody development workflows.
2. Protein-Protein Interaction Studies
The recombinant Fcer1a protein works well in pull-down assays to identify and characterize binding partners or interacting proteins from mouse cell lysates or tissue extracts. The His-SUMO tag allows efficient immobilization on nickel-based affinity matrices for capturing potential binding partners. This approach may help reveal protein complexes involving the IgE receptor alpha subunit and provide insights into receptor assembly mechanisms. The purified protein can also be applied in surface plasmon resonance or other biophysical techniques to measure binding kinetics with known interaction partners.
3. Structural and Biochemical Characterization
This recombinant protein serves as a useful tool for structural biology studies, including X-ray crystallography, NMR spectroscopy, or cryo-electron microscopy experiments aimed at understanding the molecular architecture of the IgE receptor alpha subunit. The protein can undergo various biochemical analyses such as circular dichroism spectroscopy to assess secondary structure, thermal stability assays, and proteolytic mapping studies. When native protein structure is required for certain analytical applications, the SUMO tag can be removed by specific proteases.
4. Cell-Based Binding and Functional Assays
The recombinant Fcer1a protein works as a probe in flow cytometry or microscopy-based studies to investigate receptor expression patterns on various mouse cell types. Fluorescently labeled versions of this protein may serve as reagents for detecting cells expressing complementary receptor subunits or IgE molecules. The protein can also be applied in competitive binding assays using mouse cell lines to study receptor occupancy and binding specificity under different experimental conditions.
5. ELISA Development and Immunoassay Applications
This purified recombinant protein can function as a standard or capture reagent in enzyme-linked immunosorbent assays designed to quantify Fcer1a levels in mouse biological samples. The His-SUMO tag enables oriented immobilization on ELISA plates, potentially improving assay sensitivity and reproducibility. Researchers might develop sandwich ELISA formats using this protein in combination with specific antibodies for quantitative analysis of receptor expression in cell culture supernatants or tissue homogenates.
