Analytical Data
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Gene name
IgE
- Application
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Alternative Names
IGHE; Immunoglobulin Heavy Constant Epsilon; Ig epsilon chain C region
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Species
Pig
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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
K7ZJQ0
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Expression Region
Ser1~Lys424
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Molecular Weight
50kDa
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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
Immunoglobulin E (IgE) is a key antibody involved in allergic reactions and responses to parasitic infections. The study of IgE and its recombinant forms has gained significant attention due to the increasing prevalence of allergic diseases globally, including asthma, eczema, and food allergies. Understanding the structure and function of IgE at a molecular level is crucial for developing targeted therapies and vaccines. Recombinant IgE proteins offer the potential for studying the allergenic properties of various antigens, elucidating the mechanisms of IgE-mediated signaling, and identifying novel therapeutic targets. By engineering specific IgE variants, researchers aim to investigate their binding affinities to allergens and assess their roles in triggering mast cell activation and subsequent inflammation. Furthermore, recombinant IgE can be utilized in the development of sensitive diagnostic tools for allergy detection and in the design of immunotherapies aimed at modulating IgE responses. This research is not only pivotal for advancing allergy treatments but also contributes to broader immunological insights and the potential for innovative approaches in managing immune-related disorders.
