Analytical Data
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Gene name
FceRI
- Application
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Alternative Names
FCER1A; FCE1A; FcER1 High affinity immunoglobulin epsilon receptor subunit alpha
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Species
Mouse
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P20489
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Expression Region
Ala24~Gln204
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Molecular Weight
25kDa
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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 study of recombinant FceRI (high-affinity IgE receptor) proteins is crucial for understanding allergic responses and immunological mechanisms associated with asthma and other allergic conditions. FceRI is a tetrameric receptor comprising one alpha chain, one beta chain, and two gamma chains, allowing it to bind IgE with high affinity. Upon IgE binding, FceRI initiates intracellular signaling pathways that lead to the activation of mast cells and basophils, resulting in degranulation and the release of inflammatory mediators such as histamine and leukotrienes. Given the prevalence of allergic diseases, there is a growing demand for targeted therapies that can modulate this receptor's activity. Recombinant versions of FceRI are developed to study receptor structure, function, and ligand interactions in a controlled environment. These proteins enable researchers to investigate the receptor's role in allergic sensitization and to identify potential therapeutic agents that can block IgE receptor signaling. Additionally, recombinant FceRI can be used for the development of allergen-specific immunotherapy approaches, improving our understanding of how to effectively manage allergic diseases and potentially leading to better treatment strategies. Therefore, advancements in recombinant FceRI research hold significant implications for allergy diagnostics and therapeutic interventions.
