Analytical Data
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Gene name
FceRI
- Application
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Alternative Names
FceRI;FCE1A;High affinity immunoglobulin epsilon receptor subunit alpha
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P12319
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Expression Region
1-257aa
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AA Sequence
MAPAMESPTLLCVALLFFAPDGVLAVPQKPKVSLNPPWNRIFKGENVTLT CNGNNFFEVSSTKWFHNGSLSEETNSSLNIVNAKFEDSGEYKCQHQQVNE SEPVYLEVFSDWLLLQASAEVVMEGQPLFLRCHGWRNWDVYKVIYYKDGE ALKYWYENHNISITNATVEDSGTYYCTGKVWQLDYESEPLNITVIKAPRE KYWLQFFIPLLVVILFAVDTGLFISTQQQVTFLLKIKRTRKGFRLLNPHP KPNPKNN
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Molecular Weight
54 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
The research on FcεRI (high-affinity IgE receptor) recombinant proteins has gained significant attention in immunology and allergy studies due to the critical role this receptor plays in allergic responses. FcεRI is primarily expressed on immune cells such as mast cells and basophils and is responsible for binding to IgE antibodies. When allergens cross-link the receptor-bound IgE, it triggers a series of cellular activation events, leading to the release of mediators like histamine, cytokines, and leukotrienes, which contribute to allergy symptoms and anaphylaxis. Understanding the structure and function of FcεRI is paramount for developing targeted therapies for allergic diseases, including asthma, allergic rhinitis, and food allergies. The use of recombinant proteins allows for detailed biochemical characterization and structural analysis, facilitating the delineation of receptor-ligand interactions and signaling pathways. Moreover, these recombinant proteins serve as valuable tools for vaccine development, therapeutic interventions, and diagnostic assays. By producing FcεRI in heterologous systems, researchers can study its properties in a controlled environment, leading to advancements in allergen immunotherapy and novel treatment approaches aimed at modulating the immune response to reduce the severity of allergic reactions. Thus, the investigation of FcεRI recombinant proteins holds promise for enhancing our understanding of IgE-mediated mechanisms and improving clinical outcomes for patients suffering from allergic conditions.











