|Description||The IL-2 receptor system consists of three non-covalently linked subunits termed IL-2Rα, IL-2Rβ, and IL-2Rγ. The IL-2Rα 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-2Rα releases the entire extracellular domain of IL-2Rα thereby generating a 219 amino acid soluble protein called soluble IL-2Rα (sIL-2Rα). The homodimeric form binds IL-2 (KD=10nM) and facilitates IL-2 signaling. The secreted sIL-2Rα is expressed on leukemia cells, lymphoma cells, newly activated T and B cells, as well as on approximately 10% of NK cells. Recombinant human sIL-2Rα is a 24.8 kDa protein containing 219 amino acid residues consisting of only the extracellular domain of IL-2Rα. Due to glycosylation, IL-2Rα has an approximate molecular weight of 31 kDa based on SDS-PAGE gel and Mass Spectrometry.* Manufactured using (BTI-Tn-5B1-4) cells under license from the Boyce Thompson Institute for Plant Research, Inc.|
|BiologicalActivity||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.|
|Authenticity||Verified by N-terminal and Mass Spectrometry analyses (when applicable).|
|Endotoxin||Endotoxin level is <0.1 ng/ µg of protein (<1EU/ µg).|
|Protein Content||Verified by UV Spectroscopy and/or SDS-PAGE gel.|
|Precautions||Recombinant Human sIL-2Rα is for research use only and not for use in diagnostic or therapeutic procedures.|
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