Analytical Data
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Gene name
IL-5
- Application
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Alternative Names
E-CSF; ESGF; EDF; TRF; Colony-Stimulating Factor,Eosinophil; T-Cell replacing Factor; B Cell Differentiation Factor I; Eosinophil Differentiation Factor
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Species
Dog
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Source
E. coli
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Tag
N-His
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Purity
> 97% as determined by SDS-PAGE.
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Uniprot
Q95J76
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Expression Region
Phe20~Ser134
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Molecular Weight
15kDa
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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
Interleukin-5 (IL-5) is a critical cytokine primarily produced by activated T-helper type 2 (Th2) cells and plays a significant role in regulating eosinophil production, differentiation, and activation in the immune response. Elevated levels of IL-5 are associated with various allergic conditions, including asthma, allergic rhinitis, and eosinophilic esophagitis, making it a pivotal target for therapeutic intervention. The study of recombinant IL-5 proteins has gained traction as researchers aim to understand its biological functions and signaling pathways more comprehensively. By producing IL-5 in recombinant systems, scientists can explore its interactions with specific receptors, elucidate its role in eosinophil biology, and investigate its implications in allergic diseases. Furthermore, recombinant IL-5 is also being explored for its potential use in vaccine development and as a biomarker for diagnosing and monitoring allergic conditions. The advancement of biotechnology and protein engineering techniques has paved the way for producing highly purified and biologically active IL-5, fostering research into novel therapeutic approaches aimed at modulating eosinophilic inflammation and improving patient outcomes in allergic diseases. As the understanding of IL-5 and its role in immune regulation deepens, ongoing research into its recombinant forms also aims to inform the development of more targeted therapies that may provide better efficacy and reduced side effects compared to conventional treatments.
