Analytical Data
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Gene name
IL-5
- Application
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Alternative Names
IL-5；IL5R；Interleukin-5 receptor subunit alpha
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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 primarily produced by T-helper type 2 (Th2) cells, playing a pivotal role in the regulation of eosinophil production, differentiation, and activation. Research into recombinant IL-5 was largely motivated by its significance in various eosinophil-associated diseases, including asthma, eosinophilic esophagitis, and hypereosinophilia. Elevated levels of IL-5 have been implicated in the pathophysiology of these disorders, leading to inflammation and tissue damage due to eosinophil overactivation. The development of recombinant IL-5 has facilitated the understanding of its biological functions and enabled the establishment of targeted therapies aimed at inhibiting its action. For instance, monoclonal antibodies targeting IL-5 or its receptor have been developed and are currently used as biologic treatments for severe asthma, demonstrating a marked reduction in exacerbation rates and improved lung function. Additionally, ongoing studies investigate the potential of IL-5 antagonists in treating other allergic and inflammatory conditions. The continued exploration of IL-5 and its pathways not only enhances our understanding of eosinophil biology but also provides a foundation for novel therapeutic strategies aimed at managing conditions driven by Th2 cell-mediated inflammation.
