Description: Affinity purified Rabbit polyclonal IL22 Receptor alpha 2 antibody

Description: Affinity purified Rabbit polyclonal Glycine Receptor alpha 2 antibody

Description: (IN) IL17ra (mouse) Peptide

Description: 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.

Description: 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.

Description: IL-6 mediates its biological effects through the type I IL-6 receptor system that consists of two chains, IL-6Rα and gp130. While the IL-6Rα chain is the binding component specific to IL-6, the gp130 chain only transmits signals of IL-6 when bound to IL-6Rα. The gp130 can also transmit signals from LIF, OSM, CNTF, IL-11 and CT-1 in conjunction with other receptor subunits. The low-affinity binding site for IL-6 is composed of IL-6Rα alone. IL-6Rα is expressed in a wide range of cells, including T cells, fibroblasts and macrophages. Soluble IL-6Rα, which consists of only the extracellular domain of the IL-6Rα chain, acts as an agonist of IL-6 activity at low concentrations. CHO cell-derived Recombinant Human sIL-6 Receptor α is a 37.9 kDa glycoprotein corresponding to 339 amino acid residues of the extracellular domain of IL-6Rα. As a result of glycosylation, Recombinant Human sIL-6 Receptor α migrates with an apparent molecular mass of approximately 57-70 kDa by SDS-PAGE gel, under reducing conditions.

Description: A sandwich ELISA kit for quantitative measurement of Rat IL-2R? (Interleukin 2 Receptor Alpha) in samples from Serum, Plasma, Cell supernatant

Description: A sandwich CLIA kit for quantitative measurement of Human IL-2R? (Interleukin 2 Receptor Alpha) in samples from Serum, Plasma, Cell supernatant

Description: A sandwich ELISA kit for quantitative measurement of Human IL-2R? (Interleukin 2 Receptor Alpha) in samples from Serum, Plasma, Cell supernatant