Recombinant Macaca fascicularis Interleukin-2 receptor subunit beta (IL2RB) is expressed in E. coli and contains amino acids 27 to 240 of the protein, representing a partial sequence. An N-terminal 6xHis-tag is included to simplify purification and detection processes. SDS-PAGE analysis confirms the protein achieves greater than 85% purity, which appears suitable for most research applications.
Interleukin-2 receptor subunit beta (IL2RB) serves as a key component within the interleukin-2 receptor complex. Its role in immune response regulation seems particularly important. The protein participates in signal transduction pathways that may control T cell growth, differentiation, and survival. Researchers studying immune function and therapeutic development will likely find this protein valuable for their work.
Potential Applications
Note: The applications listed below are based on what we know about this protein's biological functions, published research, and experience from experts in the field. However, we haven't fully tested all of these applications ourselves yet. We'd recommend running some preliminary tests first to make sure they work for your specific research goals.
1. Protein-Protein Interaction Studies
This recombinant IL2RB extracellular domain could help researchers examine how it binds with IL-2 cytokine and other IL-2 receptor subunits in laboratory conditions. The N-terminal His-tag allows scientists to attach the protein to nickel-coated surfaces for surface plasmon resonance (SPR) or bio-layer interferometry (BLI) experiments. These techniques measure how tightly and quickly proteins bind together. Results from such experiments might reveal important details about how IL-2 receptor complexes form in cynomolgus monkeys—information that could prove relevant for human studies since researchers often use this species in preclinical testing.
2. Antibody Development and Characterization
Scientists can use the purified IL2RB protein to create research antibodies that specifically recognize the cynomolgus monkey IL-2 receptor beta subunit. The protein also works well as a coating agent in ELISA-based screening tests to find and study monoclonal or polyclonal antibodies directed against this receptor. The His-tag makes purification and attachment steps much easier during antibody testing procedures.
3. Structural and Biochemical Analysis
This protein fragment covers the extracellular domain (amino acids 27-240), making it potentially useful for structural studies. Techniques like X-ray crystallography or NMR spectroscopy might help scientists understand the three-dimensional shape of cynomolgus IL2RB. Circular dichroism spectroscopy could assess how well the protein folds and remains stable under different laboratory conditions. Since the expression region is clearly defined, researchers can focus on analyzing the extracellular binding domain without complications from transmembrane or intracellular portions.
4. Comparative Species Analysis
Because this protein comes from Macaca fascicularis, it offers opportunities for side-by-side comparisons with human or other primate IL2RB versions. Such studies might reveal which parts of the receptor have remained the same through evolution and which differ between species. Testing how this cynomolgus protein reacts with human IL-2 or anti-human IL2RB antibodies could provide crucial information for translational research. These comparisons may be especially helpful for determining whether cynomolgus monkeys represent good models for human immune system studies, though some limitations likely exist.
