Description: The IL-2 receptor system consists of three non-covalently linked subunits termed IL-2R alpha, IL-2R beta, and IL-2R gamma.  The IL-2R alpha 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-2R alpha releases the entire extracellular domain of IL-2R alpha, thereby generating a 219 amino acid soluble protein called soluble IL-2R alpha (sIL-2R alpha).  The homodimeric form binds IL-2 (KD=10mM) and facilitates IL-2 signaling.  The secreted sIL-2R alpha 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-2R alpha. 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.

Description: The IL-2 receptor system consists of three non-covalently linked subunits termed IL-2R alpha, IL-2R beta, and IL-2R gamma.  The IL-2R alpha 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-2R alpha releases the entire extracellular domain of IL-2R alpha, thereby generating a 219 amino acid soluble protein called soluble IL-2R alpha (sIL-2R alpha).  The homodimeric form binds IL-2 (KD=10mM) and facilitates IL-2 signaling.  The secreted sIL-2R alpha 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-2R alpha. 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.

Description: A sandwich ELISA kit for quantitative measurement of Rat IL-2R? (Interleukin 2 Receptor Alpha) in samples from Serum, Plasma, Cell supernatant