Human Secreted IL-2 Receptor alpha Recombinant Protein Lyophilized from Innovative Research has been recombinantly produced in CHO cells. This is a Lyophilized protein buffered in with a purity of Greater than 98% by SDS-PAGE gel and HPLC analyses.

Endotoxin level is less than 0.1 ng per and#956;g (1EU/and#956;g)..

More Details:

• Species: Human
• Target: IL2RA
• Purity: Greater than 98% by SDS-PAGE gel and HPLC analyses.
  
  Endotoxin level is less than 0.1 ng per and#956;g (1EU/and#956;g).
• Source: CHO cells
• Storage Conditions: The lyophilized Secreted IL-2 Receptor alpha recombinant protein is stable for at least 2 years from date of receipt at -20°C. Reconstituted Secreted IL-2 Receptor alpha is stable for at least 3 months when stored in working aliquots with a carrier protein at -20°C. As with any protein, exposing Secreted IL-2 Receptor alpha recombinant protein to repeated freeze / thaw cycles is not recommended. When working with proteins care should be taken to keep recombinant protein at a cool and stable temperature.

Additional Information:

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.

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