Analytical Data
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Gene name
IL5
- Application
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Alternative Names
IL5；Interleukin-5
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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
P05113
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Expression Region
20-134aa
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AA Sequence
IPTEIPTSALVKETLALLSTHRTLLIANETLRIPVPVHKNHQLCTEEIFQ GIGTLESQTVQGGTVERLFKNLSLIKKYIDGQKKKCGEERRRVNQFLDYL QEFLGVMNTEWIIES
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Molecular Weight
13 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
Interleukin-5 (IL-5) is a cytokine that plays a crucial role in the immune system, particularly in the regulation of eosinophil growth, differentiation, and activation. Elevated levels of IL-5 have been associated with various allergic diseases and conditions, such as asthma, eosinophilic esophagitis, and hypereosinophilia. The study of recombinant IL-5 proteins has gained significant attention in the field of immunology and therapeutic research, as it facilitates the understanding of IL-5's biological functions and its potential as a therapeutic target. Researchers have been focusing on the production and characterization of recombinant IL-5 to explore its role in eosinophil-mediated inflammation and to develop targeted therapies for IL-5-associated diseases. The recombinant version allows for detailed studies on its interactions with the IL-5 receptor and the downstream signaling pathways involved in immune responses. Additionally, the development of monoclonal antibodies and other biologics targeting IL-5 has shown promise in clinical settings, demonstrating the potential of IL-5 as a therapeutic target to mitigate eosinophilic disorders. Thus, the research on IL-5 recombinant proteins not only enhances our understanding of immune regulation but also opens up avenues for innovative treatment strategies in allergic and inflammatory diseases.
