Human Recombinant sIL-2 Receptor alpha (from CHO Cells)
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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-2 Receptor alpha is a 24.8 kDa protein containing 219 amino acid residues consisting of only the extracellular domain of IL-2Ralpha. As a result of glycosylation, Recombinant Human sIL-2 Receptor alpha migrates with an apparent molecular mass of approximately 40-50 kDa by SDS-PAGE gel, under reducing and non-reducing conditions.
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