Polyclonal Antibody ; lyophilized from PBS
soluble IL-2 receptor, TAC-antigen, CD25 antigen, IL2RA; CD25; IL2R; TCGFR; IDDM10
Produced from sera of rabbits immunized with highly pure recombinant human sIL-2 Receptor alpha. Anti-Human sIL-2 Receptor alpha-specific antibody was purified by affinity chromatography employing immobilized human sIL-2 Receptor alpha as matrix.
Recombinant Human sIL-2 Receptor α (CHO cell derived)
The lyophilized antibody is stable for at least 2 years from date of receipt at -20°C. The reconstituted antibody is stable for at least two weeks at 2-8°C. Frozen aliquots are stable for at least 6 months when stored at -20°C.
Reconstitute in sterile water to a concentration of 0.1-1.0mg/mL.
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, newly activated T and B cells, as well as on approximately 10% of NK cells. Recombinant human sIL-2R alpha is a 24.8 kDa protein containing 219 amino acid residues consisting of only the extracellular domain of IL-2R alpha. Due to glycosylation, IL-2R alpha has an approximate molecular weight of 31 kDa based on SDS-PAGE gel and Mass Spectrometry.
NCBI Gene ID: