Recombinant Human IL-2 R beta Protein, CF

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. 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.

IL-2 R beta is a member of the cytokine receptor superfamily. Human IL-2 R beta cDNA encodes a 551 amino acid residue precursor Type I membrane protein with a 26 residue signal peptide, a 214 residue extracellular region, a 25 residue transmembrane region and a 286 residue cytoplasmic domain. A soluble IL-2 R beta (IL-2 sR beta ) has been identified in the culture supernatants of a human lymphoid cell line, YT, that displays IL-2 R beta . At present, the function of IL-2 sR beta is unclear. Recombinant human IL-2 sR beta 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, IL-2 sR beta binds IL-15 with sufficient affinity to neutralize IL-15 biological activities.

• 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