Analytical Data
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Gene name
IL-5Rα
- Application
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Alternative Names
IL-5Rα
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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
Q01344
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Expression Region
21-335aa
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AA Sequence
DLLPDEKISLLPPVNFTIKVTGLAQVLLQWKPNPDQEQRNVNLEYQVKIN APKEDDYETRITESKCVTILHKGFSASVRTILQNDHSLLASSWASAELHA PPGSPGTSIVNLTCTTNTTEDNYSRLRSYQVSLHCTWLVGTDAPEDTQYF LYYRYGSWTEECQEYSKDTLGRNIACWFPRTFILSKGRDWLAVLVNGSSK HSAIRPFDQLFALHAIDQINPPLNVTAEIEGTRLSIQWEKPVSAFPIHCF DYEVKIHNTRNGYLQIEKLMTNAFISIIDDLSKYDVQVRAAVSSMCREAG LWSEWSQPIYVGNDE
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Molecular Weight
38 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 receptor alpha (IL-5Rα) is a key component of the interleukin-5 (IL-5) signaling pathway, which plays a crucial role in the maturation, activation, and survival of eosinophils, a type of white blood cell involved in allergic responses and asthma. Elevated levels of IL-5 and its receptor have been implicated in various allergic disorders, making IL-5Rα a significant target for therapeutic interventions. Understanding the structure and function of IL-5Rα is essential for developing monoclonal antibodies and other biologics aimed at modulating eosinophilic activity. Recombinant IL-5Rα proteins have been generated for research purposes, allowing scientists to explore its interactions with IL-5 and potential signaling mechanisms further. These studies contribute to the identification of novel pathways and mechanisms involved in eosinophilic diseases, ultimately leading to innovative treatment options for conditions such as asthma, eosinophilic esophagitis, and chronic rhinosinusitis. The ongoing research into IL-5Rα and its role in immune responses highlights the importance of targeting eosinophils to ameliorate allergic and inflammatory diseases.
