|Calculated MW||24.8 kDa (31 kDa on SDSPAGE due to glycosylation)|
|Other Names||soluble IL-2 receptor, TAC-antigen, CD25 antigen|
|Source||(BTI-Tn-5B1-4) Hi-5 Insect Cells|
|Sequence||ELCDDDPPEI PHATFKAMAY KEGTMLNCEC KRGFRRIKSG SLYMLCTGNS SHSSWDNQCQ CTSSATRNTT KQVTPQPEEQ KERKTTEMQS PMQPVDQASL PGHCREPPPW ENEATERIYH FVVGQMVYYQ CVQGYRALHR GPAESVCKMT HGKTRWTQPQ LICTGEMETS QFPGEEKPQA SPEGRPESET SCLVTTTDFQ IQTEMAATME TSIFTTEYQ|
|Application Notes||Centrifuge the vial prior to opening. Reconstitute in 1x PBS pH 7.2 to a concentration of 0.1-1.0 mg/ml. Do not vortex. This solution can be stored at 2-8°C for up to 1 week. For extended storage, it is recommended to further dilute in a buffer containing a carrier protein (example 0.1% BSA) and store in working aliquots at -20°C to -80°C.|
|Storage||-20°C; Sterile filtered through a 0.2 micron filter. Lyophilized from 1x PBS|
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Provided below are standard protocols that you may find useful for product applications.
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=10mM) 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 SDSPAGE gel and Mass Spectrometry.
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Hayashi A.,et al.Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
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