Other Proteins

Recombinant Human IL-2 (Legacy Tebubio ref. 167200-02). IL-2 is a powerful immunoregulatory lymphokine produced by T cells in response to antigenic or mitogenic stimulation. IL-2/IL-2R signaling is required for T cell proliferation and other fundamental functions that are essential for the immune response. IL-2 stimulates growth and differentiation of B cells, NK cells, lymphokine-activated killer cells, monocytes, macrophages and oligodendrocytes. Recombinant Human IL-2 is a 15.5 kDa protein, containing 134 amino acid residues including one intrachain disulfide bond.

Recombinant Human sIL-2 Receptor alpha (CHO derived) (Legacy Tebubio ref. 167200-02RC). The IL-2 receptor system consists of three non-covalently linked subunits termed IL-2Ralpha, IL-2Rbeta, and IL-2Rgamma. The IL-2Ralpha 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-2Ralpha (sIL-2Ralpha). 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 d

Recombinant Human sIL-2 Receptor alpha (CHO derived) (Legacy Tebubio ref. 167200-02RC). The IL-2 receptor system consists of three non-covalently linked subunits termed IL-2Ralpha, IL-2Rbeta, and IL-2Rgamma. The IL-2Ralpha 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-2Ralpha (sIL-2Ralpha). 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 d

Recombinant Human sIL-4 Receptor alpha (CHO derived) (Legacy Tebubio ref. 167200-04RC). IL-4 can signal through type I and type II receptor complexes, which share a common gamma chain (gammac). The type I receptor contains, in addition to the gammac, an IL-4Ralpha subunit, whereas the type II receptor contains the IL-13Ralpha. The secreted extracellular domain of IL-4Ralpha, called sIL-4Ralpha, binds IL-4 and antagonizes its activity. It plays an important role in regulating the differentiation of naive CD4+ T cells and class switching to IgG1 and IgE. PeproTech's CHO cell-derived Recombinant Human sIL-4 Receptor alpha is a 23.9 kDa glycoprotein corresponding to 209 amino acid residues of the extracellular domain of IL-4Ralpha. As a result of glycosylation, Recombinant Human sIL-4 Receptor alpha migrates with an apparent molecular mass of approximately 50-65 kDa by SDS-PAGE gel, under reducing conditions.

Recombinant Human sIL-4 Receptor alpha (CHO derived) (Legacy Tebubio ref. 167200-04RC). IL-4 can signal through type I and type II receptor complexes, which share a common gamma chain (gammac). The type I receptor contains, in addition to the gammac, an IL-4Ralpha subunit, whereas the type II receptor contains the IL-13Ralpha. The secreted extracellular domain of IL-4Ralpha, called sIL-4Ralpha, binds IL-4 and antagonizes its activity. It plays an important role in regulating the differentiation of naive CD4+ T cells and class switching to IgG1 and IgE. PeproTech's CHO cell-derived Recombinant Human sIL-4 Receptor alpha is a 23.9 kDa glycoprotein corresponding to 209 amino acid residues of the extracellular domain of IL-4Ralpha. As a result of glycosylation, Recombinant Human sIL-4 Receptor alpha migrates with an apparent molecular mass of approximately 50-65 kDa by SDS-PAGE gel, under reducing conditions.

Recombinant Human IL-5 (Legacy Tebubio ref. 167200-05). IL-5 is a hematopoietic growth factor that stimulates the proliferation and activation of eosinophils. Produced by mast cells, T cells, and eosinophils, IL-5 plays an important role in inducing cell-mediated immunity against parasitic infections and certain tumors. Elevated levels of IL-5 lead to Eosinophilia, which may result in the induction of asthma and other allergic diseases. Human and murine IL-5 is cross-species reactive. Recombinant Human IL-5 is a 26.5 kDa disulfide-linked homodimeric protein containing two 116 amino acid chains.

Recombinant Human IL-5 (Legacy Tebubio ref. 167200-05). IL-5 is a hematopoietic growth factor that stimulates the proliferation and activation of eosinophils. Produced by mast cells, T cells, and eosinophils, IL-5 plays an important role in inducing cell-mediated immunity against parasitic infections and certain tumors. Elevated levels of IL-5 lead to Eosinophilia, which may result in the induction of asthma and other allergic diseases. Human and murine IL-5 is cross-species reactive. Recombinant Human IL-5 is a 26.5 kDa disulfide-linked homodimeric protein containing two 116 amino acid chains.

Recombinant Human sIL-6 Receptor alpha (CHO derived) (Legacy Tebubio ref. 167200-06RC). IL-6 mediates its biological effects through the type I IL-6 receptor system that consists of two chains, IL-6Ralpha and gp130. While the IL-6Ralpha chain is the binding component specific to IL-6, the gp130 chain only transmits signals of IL-6 when bound to IL-6Ralpha. 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-6Ralpha alone. IL-6Ralpha is expressed in a wide range of cells, including T cells, fibroblasts and macrophages. Soluble IL-6Ralpha, which consists of only the extracellular domain of the IL-6Ralpha chain, acts as an agonist of IL-6 activity at low concentrations. PeproTech's CHO cell-derived Recombinant Human sIL-6 Receptor alpha is a 37.9 kDa glycoprotein corresponding to 339 amino acid residues of the extracellular domain of IL-6Ralpha. As a result of gly

Recombinant Human sIL-6 Receptor alpha (CHO derived) (Legacy Tebubio ref. 167200-06RC). IL-6 mediates its biological effects through the type I IL-6 receptor system that consists of two chains, IL-6Ralpha and gp130. While the IL-6Ralpha chain is the binding component specific to IL-6, the gp130 chain only transmits signals of IL-6 when bound to IL-6Ralpha. 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-6Ralpha alone. IL-6Ralpha is expressed in a wide range of cells, including T cells, fibroblasts and macrophages. Soluble IL-6Ralpha, which consists of only the extracellular domain of the IL-6Ralpha chain, acts as an agonist of IL-6 activity at low concentrations. PeproTech's CHO cell-derived Recombinant Human sIL-6 Receptor alpha is a 37.9 kDa glycoprotein corresponding to 339 amino acid residues of the extracellular domain of IL-6Ralpha. As a result of gly