IL2RA Rabbit Polyclonal Antibody

Specifications

Product Data
Applications	ELISA, WB
Recommend Dilution	Sandwich ELISA: To detect Human sIL-2 Receptor alpha by sandwich ELISA (using 100ul/well) a concentration of 0.5-2.0 μg/ml of this antibody is required. This antigen affinity purified antibody, in conjunction with ProSci’s Biotinylated Anti-Human sIL-2 Receptor alpha as a detection antibody, allows the detection of at least 2000-4000 pg/ml of Recombinant Human sIL-2 Receptor alpha. Western Blot To detect Human sIL-2 Receptor alpha by Western Blot analysis this antibody can be used at a concentration of 0.1-0.2 μg/ml. When used in conjunction with compatible secondary reagents the detection limit for Recombinant Human sIL-2 Receptor alpha is 1.5-3.0 ng/lane, under either reducing or non-reducing conditions.
Reactivity	Human
Host	Rabbit
Clonality	Polyclonal
Immunogen	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 an immobilized Human sIL-2 Receptor alpha matrix.
Concentration	lot specific
Purification	sIL-2 Receptor alpha-specific antibody was purified by affinity chromatography employing an immobilized Human sIL-2 Receptor alpha matrix
Conjugation	Unconjugated
Storage Condition	Store at -20°C as received.
Database Link	UniProt ID P01589
Background	The IL-2 receptor system consists of three non-covalently linked subunits termed IL-2Ralpha, 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-2Ralpha releases the entire extracellular domain of IL-2Ralpha, 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-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-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.
Reference Data

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