Cytokines & Chemokines

Animal-Free Recombinant Human VEGF 165 (Legacy Tebubio ref. 167AF-100-20). VEGF is a potent growth and angiogenic cytokine. It stimulates proliferation and survival of endothelial cells, and promotes angiogenesis and vascular permeability. Expressed in vascularized tissues, VEGF plays a prominent role in normal and pathological angiogenesis. Substantial evidence implicates VEGF in the induction of tumor metastasis and intra-ocular neovascular syndromes. VEGF signals through the three receptors; fms-like tyrosine kinase (flt-1), KDR gene product (the murine homolog of KDR is the flk-1 gene product) and the flt4 gene product. Recombinant Human VEGF 165 is a 38.2 kDa, disulfide-linked homodimeric protein consisting of two 165 amino acid polypeptide chains.

Animal-Free Recombinant Human VEGF 121 (Legacy Tebubio ref. 167AF-100-20A). VEGF is a potent growth and angiogenic cytokine. It stimulates proliferation and survival of endothelial cells, and promotes angiogenesis and vascular permeability. Expressed in vascularized tissues, VEGF plays a prominent role in normal and pathological angiogenesis. VEGF signals through three receptors; fms-like tyrosine kinase (flt-1), KDR gene product (the murine homolog of KDR is the flk-1 gene product) and the flt4 gene product. Due to its increased acidity, VEGF 121 circulates more freely than other VEGF forms, which bind more tightly with vascular heparin sulfates. Recombinant Human VEGF 121 is a 28.4 kDa, disulfide-linked homodimeric protein consisting of two 121 amino acid polypeptide chains.

Animal-Free Recombinant Human VEGF 121 (Legacy Tebubio ref. 167AF-100-20A). VEGF is a potent growth and angiogenic cytokine. It stimulates proliferation and survival of endothelial cells, and promotes angiogenesis and vascular permeability. Expressed in vascularized tissues, VEGF plays a prominent role in normal and pathological angiogenesis. VEGF signals through three receptors; fms-like tyrosine kinase (flt-1), KDR gene product (the murine homolog of KDR is the flk-1 gene product) and the flt4 gene product. Due to its increased acidity, VEGF 121 circulates more freely than other VEGF forms, which bind more tightly with vascular heparin sulfates. Recombinant Human VEGF 121 is a 28.4 kDa, disulfide-linked homodimeric protein consisting of two 121 amino acid polypeptide chains.

Animal-Free Recombinant Human TGF-beta1 (CHO derived) (Legacy Tebubio ref. 167AF-100-21C). The three mammalian isoforms of TGF-beta, TGF-beta1, beta2, and beta3, signal through the same receptor and elicit similar biological responses. They are multifunctional cytokines that regulate cell proliferation, growth, differentiation and motility, as well as synthesis and deposition of the extracellular matrix. They are involved in various physiological processes, including embryogenesis, tissue remodeling and wound healing. They are secreted predominantly as latent complexes, which are stored at the cell surface and in the extracellular matrix. The release of the biologically active TGF-beta isoform from a latent complex involves proteolytic processing of the complex and/or induction of conformational changes by proteins such as thrombospondin-1. TGF-b1 is the most abundant isoform secreted by almost every cell type. It was originally identified for its ability to induce phenotypic tra

Animal-Free Recombinant Human TGF-beta1 (CHO derived) (Legacy Tebubio ref. 167AF-100-21C). The three mammalian isoforms of TGF-beta, TGF-beta1, beta2, and beta3, signal through the same receptor and elicit similar biological responses. They are multifunctional cytokines that regulate cell proliferation, growth, differentiation and motility, as well as synthesis and deposition of the extracellular matrix. They are involved in various physiological processes, including embryogenesis, tissue remodeling and wound healing. They are secreted predominantly as latent complexes, which are stored at the cell surface and in the extracellular matrix. The release of the biologically active TGF-beta isoform from a latent complex involves proteolytic processing of the complex and/or induction of conformational changes by proteins such as thrombospondin-1. TGF-b1 is the most abundant isoform secreted by almost every cell type. It was originally identified for its ability to induce phenotypic tra

Animal-Free Recombinant Human TGF-beta3 (Legacy Tebubio ref. 167AF-100-36E). The three mammalian isoforms of TGF-beta, TGF-beta1, beta2, and beta3, signal through the same receptor and elicit similar biological responses. They are multifunctional cytokines that regulate cell proliferation, growth, differentiation and motility, as well as synthesis and deposition of the extracellular matrix. They are involved in various physiological processes, including embryogenesis, tissue remodeling and wound healing. They are secreted predominantly as latent complexes, which are stored at the cell surface and in the extracellular matrix. The release of the biologically active TGF-beta isoform from a latent complex involves proteolytic processing of the complex and/or induction of conformational changes by proteins such as thrombospondin-1. The physiological role of TGF-beta3 is still unknown, but its expression pattern suggests a role in the regulation of certain development processes. Recombinant

Animal-Free Recombinant Human TGF-beta3 (Legacy Tebubio ref. 167AF-100-36E). The three mammalian isoforms of TGF-beta, TGF-beta1, beta2, and beta3, signal through the same receptor and elicit similar biological responses. They are multifunctional cytokines that regulate cell proliferation, growth, differentiation and motility, as well as synthesis and deposition of the extracellular matrix. They are involved in various physiological processes, including embryogenesis, tissue remodeling and wound healing. They are secreted predominantly as latent complexes, which are stored at the cell surface and in the extracellular matrix. The release of the biologically active TGF-beta isoform from a latent complex involves proteolytic processing of the complex and/or induction of conformational changes by proteins such as thrombospondin-1. The physiological role of TGF-beta3 is still unknown, but its expression pattern suggests a role in the regulation of certain development processes. Recombinant

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