Cytokines & Chemokines

Animal-Free Recombinant Human Growth Hormone (Legacy Tebubio ref. 167AF-100-40). Growth Hormone (GH), also known as somatotropin, is a pleiotropic cytokine of the hematopoietic growth factor superfamily, which encompasses most cytokines, hematopoietic growth factors, and related receptors, and includes the related growth hormone receptor, prolactin, placental lactogens, proliferins, and somatolactin (SST). GH is primarily recognized for its anabolic role in stimulating the growth and differentiation of muscle, bone, and cartilage. A number of other functions, including immunomodulatory actions, are also attributed to GH, due in part to the pervasive distribution of its receptors, and the indirect effects associated with GH-stimulated production of insulin-like growth factors (IGFs). Occurring predominantly in the somatotropes of the anterior pituitary, whereupon it is stored in secretory granules, production of GH has also been noted in many other tissues, including those of the hemato

Animal-Free Recombinant Human Growth Hormone (Legacy Tebubio ref. 167AF-100-40). Growth Hormone (GH), also known as somatotropin, is a pleiotropic cytokine of the hematopoietic growth factor superfamily, which encompasses most cytokines, hematopoietic growth factors, and related receptors, and includes the related growth hormone receptor, prolactin, placental lactogens, proliferins, and somatolactin (SST). GH is primarily recognized for its anabolic role in stimulating the growth and differentiation of muscle, bone, and cartilage. A number of other functions, including immunomodulatory actions, are also attributed to GH, due in part to the pervasive distribution of its receptors, and the indirect effects associated with GH-stimulated production of insulin-like growth factors (IGFs). Occurring predominantly in the somatotropes of the anterior pituitary, whereupon it is stored in secretory granules, production of GH has also been noted in many other tissues, including those of the hemato

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-17E (Legacy Tebubio ref. 167AF-200-24). IL-17E is a disulfide-linked homodimer of two 145 amino acid polypeptide chains. It belongs to the IL-17 family of structurally-related cytokines that share a highly conserved C-terminal region, but differ from one another in their N-terminal regions and in their distinct biological roles. The six known members of this family, IL-17A through IL-17F, are secreted as homodimers. IL-17E stimulates secretion of IL-8, and induces activation of the transcription factor NF-kappaB in cells that express the IL-17BR receptor. Recombinant Human IL-17E is a 33.8 kDa disulfide-linked homodimer of two 146 amino acid polypeptide chains.

Animal-Free Recombinant Human IL-17F (Legacy Tebubio ref. 167AF-200-25). IL-17F, a member of the IL-17 family of structurally related cytokines, has been shown to stimulate the proliferation and activation of T cells and PBMCs. IL-17F also regulates cartilage matrix turnover and inhibits angiogenesis. The mature human IL-17F is a homodimeric protein with a total weight of 30.1 kDa, consisting of two 133 amino acid residue chains. E.coli-derived Recombinant Human IL-17F is a biologically active, non-glycosylated, disulfide-linked homodimeric protein containing 268 amino acids (30.1 kDa), including N-terminal methionine residues.

Animal-Free Recombinant Murine IL-10 (Legacy Tebubio ref. 167AF-210-10). IL-10 is an immunosuppressive cytokine produced by a variety of mammalian cell types including macrophages, monocytes, T cells, B cells and keratinocytes. IL-10 inhibits the expression of proinflammatory cytokines such as IL-1 and TNF-alpha. Like IL-4, IL-10 enhances humoral immune responses and attenuates cell-mediated immune reactions. Human IL-10 is active on murine cells, but murine IL-10 is inactive on human cells. Recombinant Murine IL-10 is an 18.7 kDa protein of 161 amino acid residues.

Animal-Free Recombinant Murine IL-10 (Legacy Tebubio ref. 167AF-210-10). IL-10 is an immunosuppressive cytokine produced by a variety of mammalian cell types including macrophages, monocytes, T cells, B cells and keratinocytes. IL-10 inhibits the expression of proinflammatory cytokines such as IL-1 and TNF-alpha. Like IL-4, IL-10 enhances humoral immune responses and attenuates cell-mediated immune reactions. Human IL-10 is active on murine cells, but murine IL-10 is inactive on human cells. Recombinant Murine IL-10 is an 18.7 kDa protein of 161 amino acid residues.

Animal-Free Recombinant Murine IL-21 (Legacy Tebubio ref. 167AF-210-21). IL-21 is a pleiotropic cytokine produced by CD4+ T cells in response to antigenic stimulation. Its action generally enhances antigen-specific responses of immune cells. The biological effects of IL-21 include: inducing the differentiation of T cell-stimulated B cells into plasma cells and memory B cells; the stimulation of IgG production in conjunction with IL-4; and the induction of apoptotic effects in naive B cells and stimulated B cells in the absence of T-cell signaling. Additionally, IL-21 promotes the anti-tumor activity of CD8+ T cells and NK cells. IL-21 exerts its effect through binding to a specific type I cytokine receptor, IL-21R, which also contains the gamma chain (gammac) found in other cytokine receptors, including IL-2, IL-4, IL-7, IL-9 and IL-15. The IL-21/IL-21R interaction triggers a cascade of events, which includes activation of the tyrosine kinases JAK1 and JAK3, followed by activation of t