Recombinant Human IL-2 R beta Fc Chimera Protein, CF

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

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. 

Array 10919-2B

• IL-2 R beta Antibodies
• IL-2 R beta ELISA Kits
• IL-2 R beta Lysate
• IL-2 R beta Protein
• IL-2 R beta Proteins and Enzymes