Cytokines & Chemokines

Animal-Free Recombinant Human/Murine/Rat BMP-2 (E.coli derived) (Legacy Tebubio ref. 167AF-120-02). BMPs (Bone Morphogenetic Proteins) belong to the TGF-beta superfamily of structurally related signaling proteins. BMP-2 is a potent osteoinductive cytokine, capable of inducing bone and cartilage formation in association with osteoconductive carriers such as collagen and synthetic hydroxyapatite. In addition to its osteogenic activity, BMP-2 plays an important role in cardiac morphogenesis, and is expressed in a variety of tissues, including lung, spleen, brain, liver, prostate, ovary, and small intestine. The functional form of BMP-2 is a 26 kDa protein composed of two identical 114 amino acid polypeptide chains linked by a single disulfide bond. Each BMP-2 monomer is expressed as the C-terminal part of a precursor polypeptide, which also contains a 23 amino acid signal sequence for secretion, and a 259 amino acid propeptide. After dimerization of this precursor, the covalent bonds betw

Animal-Free Recombinant Human/Murine/Rat BMP-2 (E.coli derived) (Legacy Tebubio ref. 167AF-120-02). BMPs (Bone Morphogenetic Proteins) belong to the TGF-beta superfamily of structurally related signaling proteins. BMP-2 is a potent osteoinductive cytokine, capable of inducing bone and cartilage formation in association with osteoconductive carriers such as collagen and synthetic hydroxyapatite. In addition to its osteogenic activity, BMP-2 plays an important role in cardiac morphogenesis, and is expressed in a variety of tissues, including lung, spleen, brain, liver, prostate, ovary, and small intestine. The functional form of BMP-2 is a 26 kDa protein composed of two identical 114 amino acid polypeptide chains linked by a single disulfide bond. Each BMP-2 monomer is expressed as the C-terminal part of a precursor polypeptide, which also contains a 23 amino acid signal sequence for secretion, and a 259 amino acid propeptide. After dimerization of this precursor, the covalent bonds betw

Animal-Free Recombinant Human IL-1alpha (Legacy Tebubio ref. 167AF-200-01A). 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-200-01A). 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-200-01B). 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.

Animal-Free Recombinant Human IL-1beta (Legacy Tebubio ref. 167AF-200-01B). 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.

Animal-Free Recombinant Human IL-3 (Legacy Tebubio ref. 167AF-200-03). IL-3 is a hematopoietic growth factor that promotes the survival, differentiation and proliferation of committed progenitor cells of the megakaryocyte, granulocyte-macrophage, erythroid, eosinophil, basophil and mast cell lineages. Produced by T cells, mast cells and eosinophils, IL-3 enhances thrombopoiesis, phagocytosis, and antibody-mediated cellular cytotoxicity. Its ability to activate monocytes suggests that IL-3 may have additional immunoregulatory roles. Many of the IL-3 activities depend upon co-stimulation with other cytokines. IL-3 is a species-specific, variably glycosylated cytokine. Recombinant Human IL-3 is a 15.0 kDa globular protein containing 133 amino acid residues.

Animal-Free Recombinant Human IL-3 (Legacy Tebubio ref. 167AF-200-03). IL-3 is a hematopoietic growth factor that promotes the survival, differentiation and proliferation of committed progenitor cells of the megakaryocyte, granulocyte-macrophage, erythroid, eosinophil, basophil and mast cell lineages. Produced by T cells, mast cells and eosinophils, IL-3 enhances thrombopoiesis, phagocytosis, and antibody-mediated cellular cytotoxicity. Its ability to activate monocytes suggests that IL-3 may have additional immunoregulatory roles. Many of the IL-3 activities depend upon co-stimulation with other cytokines. IL-3 is a species-specific, variably glycosylated cytokine. Recombinant Human IL-3 is a 15.0 kDa globular protein containing 133 amino acid residues.

Animal-Free Recombinant Human IL-4 (Legacy Tebubio ref. 167AF-200-04). IL-4 is a pleiotropic cytokine that regulates diverse T and B cell responses including cell proliferation, survival and gene expression. Produced by mast cells, T cells and bone marrow stromal cells, IL-4 regulates the differentiation of naive CD4+ T cells into helper Th2 cells, characterized by their cytokine-secretion profile that includes secretion of IL-4, IL-5, IL-6, IL-10, and IL-13, which favor a humoral immune response. Another dominant function of IL-4 is the regulation of immunoglobulin class switching to the IgG1 and IgE isotypes. Excessive IL-4 production by Th2 cells has been associated with elevated IgE production and allergy. Recombinant Human IL-4 is a 15.1 kDa globular protein containing 130 amino acid residues.