Cytokines & Chemokines

Recombinant Human sIL-23 Receptor Fc (Legacy Tebubio ref. 167200-23R). IL-23R is a 629 aa, novel subunit of the receptor for cytokine IL23A/IL23 which pairs with the receptor molecule IL12RB1/IL12R beta 1and thus take part in IL23A signaling. Signal transduction analysis confirms that this protein associates constitutively with Janus kinase 2 (JAK2), and also binds to transcription activator STAT3 in a ligand-dependent manner. Alternative splicing results in six spliced isoforms of IL-23R. Reports suggest that IL-23R plays an important role in psoriasis pathogenesis and is also a potential therapeutic target in inflammatory bowel disease. Recombinant Human IL-23 Receptor Fc is a 128.2 kDa homodimeric protein of 1128 amino acids, consisting of the extracellular domain of the mature sequence, as well as a 230-residue C-terminal Fc region linked by two glycines. As a result of glycosylation the Recombinant Human IL-23 Receptor Fc migrates to an apparent molecular weight slightly above 200

Recombinant Human sIL-23 Receptor Fc (Legacy Tebubio ref. 167200-23R). IL-23R is a 629 aa, novel subunit of the receptor for cytokine IL23A/IL23 which pairs with the receptor molecule IL12RB1/IL12R beta 1and thus take part in IL23A signaling. Signal transduction analysis confirms that this protein associates constitutively with Janus kinase 2 (JAK2), and also binds to transcription activator STAT3 in a ligand-dependent manner. Alternative splicing results in six spliced isoforms of IL-23R. Reports suggest that IL-23R plays an important role in psoriasis pathogenesis and is also a potential therapeutic target in inflammatory bowel disease. Recombinant Human IL-23 Receptor Fc is a 128.2 kDa homodimeric protein of 1128 amino acids, consisting of the extracellular domain of the mature sequence, as well as a 230-residue C-terminal Fc region linked by two glycines. As a result of glycosylation the Recombinant Human IL-23 Receptor Fc migrates to an apparent molecular weight slightly above 200

Recombinant Murine sIL-33 Receptor FC (Legacy Tebubio ref. 167210-33R). IL-33R, also known as ST2, is a receptor for IL-33. It is a member of the IL-1 receptor family of innate receptors. Its extracellular domain consists of 3 Ig-like domains that directly interact with its co-receptor IL-1RAcP, and the ligand alarmin, IL-33. IL-33 ligation results in the association of IL-33R complex with its adaptor proteins MyD88, IRAK1, IRAK4 and TRAF6, and activation of the NF-κB, and MAPK pathways. This, in turn, instigates the release of chemokines and cytokines such as IL-5, IL-6, IL-8, and IL-13. Two most common isoforms of IL-33R that result from alternative splicing are ST2L – the membrane bound form, and ST2S – the soluble form. The membrane bound form can be released from the cell surface by proteolytic cleavage. The soluble forms have been suggested to act as decoys dampening the IL-33 signaling. IL-33R is primarily expressed by mast cells, basophils, and eosinophils. In mice, IL-33R expr

Recombinant Murine sIL-33 Receptor FC (Legacy Tebubio ref. 167210-33R). IL-33R, also known as ST2, is a receptor for IL-33. It is a member of the IL-1 receptor family of innate receptors. Its extracellular domain consists of 3 Ig-like domains that directly interact with its co-receptor IL-1RAcP, and the ligand alarmin, IL-33. IL-33 ligation results in the association of IL-33R complex with its adaptor proteins MyD88, IRAK1, IRAK4 and TRAF6, and activation of the NF-κB, and MAPK pathways. This, in turn, instigates the release of chemokines and cytokines such as IL-5, IL-6, IL-8, and IL-13. Two most common isoforms of IL-33R that result from alternative splicing are ST2L – the membrane bound form, and ST2S – the soluble form. The membrane bound form can be released from the cell surface by proteolytic cleavage. The soluble forms have been suggested to act as decoys dampening the IL-33 signaling. IL-33R is primarily expressed by mast cells, basophils, and eosinophils. In mice, IL-33R expr

Recombinant Human Vista Fc (Legacy Tebubio ref. 167310-45). VISTA (V-domain Ig containing suppressor of T-cell activation), also known as B7-H5 or PD-1H, is a product of the VSIR gene. Although VISTA bears sequence homology to PD-L1 it has a different expression pattern. In both mouse and humans, VISTA is expressed predominantly on hematopoietic cells with the highest densities on myeloid cells, and lower levels on T cells. It is usually absent on B cells. VISTA expressed by antigen presenting cells has been shown to directly suppress proliferation and cytokine production of CD4 and CD8 T cells, making it a target for cancer immunotherapy. The reported ligands of VISTA include CD28H, VSIG-3 and VSIG-8. Recombinant Human VISTA Fc is a 88.2 kDa homodimeric protein of 395 amino acids consisting of the extracellular domain of the mature sequence, as well as a 230-residue C-terminal Fc region linked by two glycines. As a result of glycosylation, the Recombinant Human VISTA Fc migrates to an

Recombinant Human Vista Fc (Legacy Tebubio ref. 167310-45). VISTA (V-domain Ig containing suppressor of T-cell activation), also known as B7-H5 or PD-1H, is a product of the VSIR gene. Although VISTA bears sequence homology to PD-L1 it has a different expression pattern. In both mouse and humans, VISTA is expressed predominantly on hematopoietic cells with the highest densities on myeloid cells, and lower levels on T cells. It is usually absent on B cells. VISTA expressed by antigen presenting cells has been shown to directly suppress proliferation and cytokine production of CD4 and CD8 T cells, making it a target for cancer immunotherapy. The reported ligands of VISTA include CD28H, VSIG-3 and VSIG-8. Recombinant Human VISTA Fc is a 88.2 kDa homodimeric protein of 395 amino acids consisting of the extracellular domain of the mature sequence, as well as a 230-residue C-terminal Fc region linked by two glycines. As a result of glycosylation, the Recombinant Human VISTA Fc migrates to an

Animal-Free Recombinant Human IL-1alpha (Legacy Tebubio ref. 167AF-01A). IL-1alpha is a non-secreted, proinflammatory cytokine produced in a variety of cells, including monocytes, tissue macrophages, keratinocytes, and other epithelial cells. Both IL-1alpha and IL-1beta bind to the same receptor and have similar, if not identical, biological properties. These cytokines have a broad range of activities including the stimulation of thymocyte proliferation by inducing IL-2 release, Bcell maturation and proliferation, mitogenic FGF-like activity and the release of prostaglandin and collagenase from synovial cells. However, whereas IL-1beta is a secreted cytokine, IL-1alpha is predominantly a cell-associated cytokine. Recombinant Human IL-1alpha is an 18.0 kDa protein containing 159 amino acid residues.

Animal-Free Recombinant Human IL-1alpha (Legacy Tebubio ref. 167AF-01A). IL-1alpha is a non-secreted, proinflammatory cytokine produced in a variety of cells, including monocytes, tissue macrophages, keratinocytes, and other epithelial cells. Both IL-1alpha and IL-1beta bind to the same receptor and have similar, if not identical, biological properties. These cytokines have a broad range of activities including the stimulation of thymocyte proliferation by inducing IL-2 release, Bcell maturation and proliferation, mitogenic FGF-like activity and the release of prostaglandin and collagenase from synovial cells. However, whereas IL-1beta is a secreted cytokine, IL-1alpha is predominantly a cell-associated cytokine. Recombinant Human IL-1alpha is an 18.0 kDa protein containing 159 amino acid residues.

Animal-Free Recombinant Human IL-1beta (Legacy Tebubio ref. 167AF-01B). IL-1beta is a proinflammatory cytokine produced in a variety of cells, including monocytes, tissue macrophages, keratinocytes, and other epithelial cells. Both IL-1alpha and IL-1beta bind to the same receptor and have similar, if not identical, biological properties. These cytokines have a broad range of activities including the stimulation of thymocyte proliferation by inducing IL-2 release, B cell maturation and proliferation, mitogenic FGF-like activity, and the release of prostaglandin and collagenase from synovial cells. However, whereas IL-1beta is a secreted cytokine, IL-1alpha is predominantly a cell-associated cytokine. Recombinant Human IL-1beta is a 17.3 kDa protein containing 153 amino acid residues.