Interleukin-2 (IL-2) is a pluripotent cytokine which plays a crucial role in the immune system response. And the IL-2 receptor (IL-2R) is a heterotrimeric protein expressed on the surface of certain immune cells, such as lymphocytes, that binds and responds to IL-2.
IL-2R consists of three subunits, namely IL-2Rα (CD25), IL-2Rβ (CD122), and common γc (CD132). The three receptor chains are expressed separately and differently on various cell types and can assemble in different combinations and orders to generate low, intermediate, and high affinity IL-2 receptors.
Many biopharma and biotech companies have carried out different IL-2 modification and design, including PEG modification, fusion FC, IL-2 mutant design, bispecific antibody design, and combined immunization checkpoint antibody drug therapy and other strategies.
Therefore, a series of structurally stable and high-affinity IL-2 receptor heterodimers and heterotrimers are of great significance for in vitro studies of the interaction between IL-2 and IL-2 receptors, and also for the antibody immunization and screening.
Fig.1 Native IL-2 has pleiotropic effects on the immune response
Fig 2. Schematic of IL-2 binding to the low-affinity, intermediate-affinity and high-affinity IL-2 receptors. The high-affinity receptor comprises IL-2 receptor α-chain (IL-2Rα), IL-2Rβ and IL-2Rγ.
ACROBiosystems has developed a variety of exclusive IL-2 R alpha, IL-2 R beta & IL-2 R gamma heterotrimeric proteins and IL-2 R beta & IL-2 R gamma heterodimer proteins using its own patented technology. These products are HEK 293 expressed with special design, making them more stable and higher consistency among batches and solving the instability and inconvenience in traditional in vitro assemble methods. In addition, the high purity and affinity were verified by MALS and SPR respectively, and protocols are available for free. We believe that the featured heteropolymers can play a critical role in in vitro studies of the interaction between IL-2 and IL-2 receptors, and also for the antibody immunization and screening.
Table 1 Affinity of IL-2 binding to IL-2R (SPR)
Affinity to Human IL-2
Human IL-2RB&IL-2RA&IL-2RG, Fc Tag&Fc Tag (Cat. No. ILG-H5257) captured on CM5 chip via Anti-human IgG Fc antibodies surface can bind Human IL-2, Tag Free (Cat. No. IL2-H4113) with an affinity constant of 40.6 pM as determined in a SPR assay (Biacore 8K).
Human IL-2 R alpha, His Tag (Cat. No. ILA-H52H9) captured on CM5 chip via anti-His antibody, can bind Human IL-2, Tag Free (Cat. No. IL2-H4113) with an affinity constant of 29.9 nM as determined in a SPR assay (Biacore T200).
The purity of Human IL-2RB&IL-2RG Heterodimer Protein, Fc Tag&Fc Tag (MALS verified)(Cat. No. ILG-H5254) was more than 90% and the molecular weight of this protein is around 145-165 kDa verified by SEC-MALS.
The purity of Human IL-2RB&IL-2RA&IL-2RG, Fc Tag&Fc Tag(Cat. No. ILG-H5257) was more than 90% and the molecular weight of this protein is around 175-190 kDa verified by SEC-MALS.
Immobilized Human IL-2, Tag Free (Cat. No. IL2-H4113) at 5 μg/mL (100 μL/well) can bind Human IL-2RB&IL-2RG Heterodimer Protein, Fc Tag&Fc Tag (MALS verified) (Cat. No. ILG-H5254) with a linear range of 5-78 ng/mL
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