Analytical Data
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Gene name
Fc epsilon RIA/FCER1A
- Application
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Alternative Names
Fc-epsilon RI-alpha Short name: FcERI IgE Fc receptor subunit alpha
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Species
Human
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Source
Yeast
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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
P12319
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Expression Region
26-205aa
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Molecular Weight
23 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
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Protein Description
Fc epsilon receptor I alpha (FcεRIα) is a crucial protein involved in IgE-mediated allergic responses and is primarily found on the surface of mast cells and basophils. The engagement of IgE with FcεRIα leads to cell activation and the release of histamines and other mediators contributing to allergic diseases such as asthma, allergic rhinitis, and anaphylaxis. Understanding the structure and function of FcεRIα is essential for developing novel therapeutic strategies to manage allergic conditions. Recombinant FcεRIα protein serves as a valuable tool for investigating the molecular mechanisms underlying IgE signaling and receptor activation. It also facilitates the study of FcεRIα interactions with various ligands and monoclonal antibodies, which may lead to the identification of potential therapeutic inhibitors or modulators of allergic responses. Moreover, the characterization of recombinant FcεRIα contributes to the design of specific immunoassays for diagnosing allergy-related disorders. Overall, research on FcεRIα and its recombinant forms is pivotal for advancing our knowledge of allergic reactions and improving clinical approaches to allergy management.
