Recombinant Human IL-2 R beta Fc Chimera Protein, CF Summary
|Human IL-2 R beta |
Accession # P14784.1
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CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.|
|Reconstitution||Reconstitute at 250 μg/mL in PBS.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
Recombinant Human IL‑2 R beta Fc Chimera (Catalog # 10919-2B) inhibits Recombinant Human IL-15 (247-ILB) dependent proliferation of MO7e human megakaryocytic leukemic cells. The ED50 for this effect is 1.75-14.0 μg/mL.
2 μg/lane of Recombinant Human IL‑2 R beta Fc Chimera Protein (Catalog # 10919-2B) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 62-68 kDa and 120-140 kDa, respectively.
Background: IL-2 R beta
Interleukin-2 receptor subunit beta (IL-2 RB), also known as high affinity IL-2 receptor subunit beta, interleukin-15 receptor subunit beta, p70-75 (p75), and CD122, is a member of the cytokine receptor superfamily that plays a role in T cell-mediated immune responses (1, 3). Human IL-2 RB consists of an extracellular domain (ECD) containing a fibronectin type III domain and a WSXWS motif, a type I transmembrane domain, and a cytoplasmic tail. Within the ECD, mature human IL-2 RB shares 58% and 61% amino acid sequence identity with mouse and rat IL-2 RB, respectively. A soluble IL-2 RB (sIL-2 RB) has been identified in the culture supernatants of a human lymphoid cell line, YT, that displays IL-2 RB (5). Functional IL-2 receptors can exist in two affinity states on cell surfaces: the high affinity complex consisting of heterotrimers of the alpha, beta, and gamma chains and the intermediate affinity complex comprising heterodimers of the beta and gamma chains (2, 3). Individual beta chains and alpha chains exhibit low affinity IL-2 binding and the gamma chain alone does not bind IL-2. In addition to their involvement in IL-2 mediated signal transduction, both the beta chain and gamma chain have been shown to be required for IL-15 mediated signaling (4). At present, the function of IL-2 sR beta is unclear. Recombinant human sIL-2RB binds IL-2 with low affinity and is not an effective IL-2 antagonist on cells displaying the high or intermediate affinity IL-2 signaling receptors. Nevertheless, sIL-2 RB binds IL-15 with sufficient affinity to neutralize IL-15 biological activities.
- Jia, Z. et al. (2019) Int. Immunpharmacol. 74:105716.
- Zhou, X. et al. (2019) Fish & Shellfish Immunol. 93:641.
- Zhang, Z. et al. (2019) J. Exp. Med. 216:1311.
- Fernandez, I. et al. (2019) J. Exp. Med. 216:1255.
- Honda, M. et al. (1990) J. Immunol. 145:4131.
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