Analytical Data
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Gene name
IL-2R beta/CD122
- Application
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Alternative Names
CD122; IL2R-b; IL2-RB; P70-75; High affinity IL-2 receptor subunit beta; Interleukin-2 receptor subunit beta; IL-2 receptor subunit beta
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by reducing SDS-PAGE.
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Uniprot
P14784
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Expression Region
Ala27~Thr240
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Molecular Weight
28kDa
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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-2 receptor beta (IL-2Rβ/CD122) is a crucial component of the IL-2 receptor complex, which plays an essential role in the modulation of immune responses. This receptor is primarily expressed on activated T cells and natural killer (NK) cells and is involved in mediating the effects of interleukin-2 (IL-2), a key cytokine for T cell proliferation, differentiation, and survival. Research into IL-2Rβ/CD122 has gained prominence due to its implications in various immunological disorders, including autoimmune diseases, cancer, and infections. The receptor exists in different forms, including a high-affinity complex with IL-2Rα (CD25) and a lower-affinity form in conjunction with the common gamma chain (CD132). This diversity allows for fine-tuning of immune responses, making it a target for therapeutic interventions. Recombinant forms of IL-2Rβ/CD122 have been produced for both functional studies and potential clinical applications, including the development of novel immunotherapies. Understanding the structure and function of this receptor is essential for designing effective treatments that enhance immune responses or mitigate excessive inflammation. Thus, the continued exploration of IL-2Rβ/CD122 as a therapeutic target holds promise for advancing strategies to manipulate the immune system in various diseases.
