Analytical Data
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Gene name
IL-4R alpha/CD124
- Application
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Alternative Names
CD124; IL-4 R alpha; IL-4R subunit alpha; IL4R; IL-4Ra; IL4RACD124
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Species
Canine
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Source
HEK293
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Tag
C-8*His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
XP_035573985.2
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Expression Region
G24-H231
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Protein Length
Partial
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Molecular Weight
50-65 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
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Protein Description
Interleukin-4 receptor alpha (IL-4Rα or CD124) is a crucial component of the immune system, primarily involved in mediating the effects of interleukin-4 (IL-4) and interleukin-13 (IL-13), two cytokines that play significant roles in allergic responses, asthma, and other inflammatory diseases. The heterodimeric receptor consists of IL-4Rα and the common gamma chain (γc), facilitating various signal transduction pathways that influence immune cell differentiation, proliferation, and cytokine production. Research on IL-4Rα/CD124 recombinant proteins has gained momentum due to their potential therapeutic applications in modulating immune responses. By utilizing recombinant DNA technology, researchers can produce these proteins in cultured cells, allowing for the study of their biological functions and interactions with ligands. This has implications for designing novel therapeutic strategies targeting IL-4Rα to mitigate chronic inflammatory conditions or modify immune responses in diseases like cancer. Furthermore, understanding the structural dynamics and binding affinities of IL-4Rα in complex with its ligands may pave the way for the development of small molecule inhibitors or monoclonal antibodies aimed at blocking its activity, offering new avenues for treatment. As such, the study of IL-4Rα/CD124 recombinants not only enhances our understanding of immune regulation but also holds promise for innovation in clinical interventions against a range of immune-related disorders.
