Analytical Data
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Gene name
Fc epsilon RIA/FCER1A
- Application
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Alternative Names
Fc-epsilon RI-alpha
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Species
Mouse
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Source
E. coli
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Tag
N- His-SUMO
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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
24-250aa
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Molecular Weight
44.7 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
Fc epsilon receptor I (FcεRI) and its corresponding gene FCER1A play crucial roles in the immune response, particularly in allergic reactions and asthma. FcεRI is a high-affinity receptor for immunoglobulin E (IgE), which is pivotal in mediating allergic responses to environmental allergens. The activation of FcεRI on mast cells and basophils leads to the degranulation of these cells, releasing various inflammatory mediators such as histamines, leukotrienes, and cytokines, which contribute to the symptoms of allergic diseases. Understanding the structure and function of the FcεRI receptor, particularly through the study of recombinant FCER1A proteins, offers valuable insights into the mechanisms of IgE-mediated signaling pathways. This research is vital for developing targeted therapeutic strategies to manage allergic conditions by potentially blocking or modulating the receptor's activity. Furthermore, the examination of FcεRI can also aid in identifying biomarkers for allergic diseases, improving diagnostic tools, and enhancing the efficacy of existing treatments. The ongoing studies on the recombinant forms of FCER1A thus hold promise for advancing our knowledge and treatment of IgE-related disorders.
