Analytical Data
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Gene name
IgE
- Application
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Alternative Names
IgE；Immunoglobulin heavy constant epsilon
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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
P0DOX4
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Expression Region
1-547aa
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AA Sequence
QVQLVQSGAEVRKPGASVRVSCKASGYTFIDSYVGWIRQAPGHGLEWIHWINPNSGGTNYAPRFQGRVTMTRDASFSTAYMDLRSLRSDDSAVFYCAKSDPFWSDYNFDYSSSEEGTEVTYTVSGAWTLPSVFPLTRCCKNIPSNATSVTLGCLATGYFPEPVMVTWDTGSLNGTTLPATTLTLSGHYATISLLTVSGAWAKQMFTCRVAHTPSSTVDNKTFSVCSRDFTPPTVKILQSSCDGLGHFPPTIQLCLVSGYTPGTINITWLEDGQVMDVDLSTASTESQGELASTESQLTLSQKHWLSDRTYTCQVTYQGHTFQDSTKKCADSNPRGVSAYLSRPSPFDLFIRKSPTITCLVVDLAPSKGTVNLTWSRASGKPVNHSTRKEEKQRNGTLTVTSTLPVGTRDWIEGETYQCRVTHPHLPRALMRSTTKTSGPRAAPEVYAFATPEWPGSRDKRTLACLIQNFMPEDISVQWLHNEVQLPDARHSTTQPRKTKGSGFFVFSRLEVTRAEWQEKDEFICRAVHEAASPSQTVQRAVSVNPGK
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Molecular Weight
60.3 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
Immunoglobulin E (IgE) plays a critical role in allergic reactions and is associated with various allergic diseases, including asthma, hay fever, and food allergies. The study of IgE and its recombinant proteins has garnered significant attention in recent years due to the increasing prevalence of allergic conditions worldwide. Traditional therapeutic approaches have focused on symptom management rather than addressing the underlying immune response. Consequently, researchers have turned to recombinant IgE proteins to better understand its structure, function, and interaction with allergens and Fc receptors. Recombinant technologies facilitate the production of specific IgE variants, enabling detailed studies on their bioactivity and potential as targets for novel allergy treatments. Additionally, these proteins can be utilized to create targeted therapies, such as monoclonal antibodies, which can inhibit IgE binding or block its function, offering hope for more effective allergy management. Understanding the intricacies of IgE behavior at a molecular level may lead to breakthroughs in immunotherapy and allergy prevention strategies, making IgE recombinant proteins a focal point of modern immunological research.
