Description
Human, Mouse sIL-2 Receptor a Recombinant Protein Lyophilized has been recombinantly produced in (BTI-Tn-5B1-4) High-5 Insect cells.
The IL-2 receptor system consists of three non-covalently linked subunits termed IL-2Ralpha, IL-2Rbeta, and IL-2Rgamma. The IL-2Ralpha is a type I transmembrane protein consisting of a 219 amino acid extracellular domain, a 19 amino acid transmembrane domain and a 13 amino acid intracellular domain, which is not involved in the transduction of IL-2 signals. Proteolytic processing of IL-2Ralpha releases the entire extracellular domain of IL-2Ralpha, thereby generating a 219 amino acid soluble protein called soluble IL-2Ralpha (sIL-2Ralpha). The homodimeric form binds IL-2 (KD=10mM) and facilitates IL-2 signaling. The secreted sIL-2Ralpha is expressed on leukemia cells, lymphoma cells, and newly activated T and B cells, as well as on approximately 10% of NK cells. Recombinant Human sIL-2Ralpha is a 24.8 kDa protein containing 219 amino acid residues consisting of only the extracellular domain of IL-2Ralpha. Due to glycosylation, IL-2Ralpha has an approximate molecular weight of 31 kDa based on SDS-PAGE gel and Mass Spectrometry