Recombinant Human sIL-2 Receptor Alpha (CHO derived)(Discontinued)

Source:CHO 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-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.

Determined by its ability to increase the proliferation effect of IL-2 in murine CTLL-2 cells. In the presence of 1 ng/ml of recombinant IL-2, the expected ED₅₀ for this effect is between 0.5 - 1.5 µg/ml.

For Research Use Only. Not for use in diagnostic/therapeutics procedures.

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