Cytokines & Chemokines

Animal-Free Recombinant Human IL-17A (Legacy Tebubio ref. 167AF-200-17). The originally described IL-17 protein, now known as IL-17A, is a homodimer of two 136 amino acid chains that are secreted by activated T-cells, which act on stromal cells to induce production of proinflammatory and hematopoietic bioactive molecules. Today, IL-17 represents a 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-17A exhibits cross-species bioactivity between human and murine cells. Recombinant Human IL-17A is a 31.3 kDa, disulfide-linked homodimer of two 137 amino acid, polypeptide chains.

Animal-Free Recombinant Human IL-21 (Legacy Tebubio ref. 167AF-200-21). 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 th

Animal-Free Recombinant Human IL-21 (Legacy Tebubio ref. 167AF-200-21). 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 th

Animal-Free Recombinant Human IL-22 (Legacy Tebubio ref. 167AF-200-22). IL-22 is a member of the IL-10 family of regulatory cytokines, which includes IL-10, IL-19, IL-20, IL-22, IL-24 and IL-26. Members of this family share partial homology in their amino acid sequences, but they are dissimilar in their biological functions. Produced by T lymphocytes, IL-22 inhibits IL-4 production by Th2 cells, and induces acute phase reactants in the liver and pancreas. IL-22 signals through a receptor system consisting of IL-10Rbeta/CRF2-4 and IL-22R, both of which are members of the class II cytokine-receptor family. Recombinant Human IL-22 is a 33.6 kDa, non-disulfide-linked, homodimeric protein consisting of two 147 amino acid polypeptide chains.

Animal-Free Recombinant Human IL-22 (Legacy Tebubio ref. 167AF-200-22). IL-22 is a member of the IL-10 family of regulatory cytokines, which includes IL-10, IL-19, IL-20, IL-22, IL-24 and IL-26. Members of this family share partial homology in their amino acid sequences, but they are dissimilar in their biological functions. Produced by T lymphocytes, IL-22 inhibits IL-4 production by Th2 cells, and induces acute phase reactants in the liver and pancreas. IL-22 signals through a receptor system consisting of IL-10Rbeta/CRF2-4 and IL-22R, both of which are members of the class II cytokine-receptor family. Recombinant Human IL-22 is a 33.6 kDa, non-disulfide-linked, homodimeric protein consisting of two 147 amino acid polypeptide chains.

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-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 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.