Cytokines & Chemokines

Animal-Free Recombinant Human IL-13 (Legacy Tebubio ref. 167AF-13). IL-13 is an immunoregulatory cytokine produced primarily by activated Th2 cells, and also by mast cells and NK cells. Targeted deletion of IL-13 in mice resulted in impaired Th2 cell development and indicated an important role for IL-13 in the expulsion of gastrointestinal parasites. IL-13 exerts anti-inflammatory effects on monocytes and macrophages and it inhibits the expression of inflammatory cytokines such as IL-1beta, TNF-alpha, IL-6 and IL-8. IL-13 has also been shown to enhance B cell proliferation and to induce isotype switching, resulting in increased production of IgE. Blocking of IL-13 activity inhibits the pathophysiology of asthma. Human and murine IL-13 are cross-species reactive. Recombinant Human IL-13 is a 12.6 kDa protein consisting of 115 amino acid residues.

Animal-Free Recombinant Human IL-13 (Legacy Tebubio ref. 167AF-13). IL-13 is an immunoregulatory cytokine produced primarily by activated Th2 cells, and also by mast cells and NK cells. Targeted deletion of IL-13 in mice resulted in impaired Th2 cell development and indicated an important role for IL-13 in the expulsion of gastrointestinal parasites. IL-13 exerts anti-inflammatory effects on monocytes and macrophages and it inhibits the expression of inflammatory cytokines such as IL-1beta, TNF-alpha, IL-6 and IL-8. IL-13 has also been shown to enhance B cell proliferation and to induce isotype switching, resulting in increased production of IgE. Blocking of IL-13 activity inhibits the pathophysiology of asthma. Human and murine IL-13 are cross-species reactive. Recombinant Human IL-13 is a 12.6 kDa protein consisting of 115 amino acid residues.

Animal-Free Recombinant Human IL-15 (Legacy Tebubio ref. 167AF-15). IL-15 is an immunomodulating cytokine that stimulates the proliferation of T lymphocytes and shares many biological properties with IL-2. IL-15 exerts its biological activities primarily on T cells. It is also essential in the development, survival and activation of NK cells. Increased expression of IL-15 has been linked to rheumatoid arthritis, inflammatory bowel disease, and diseases affiliated with retroviruses HIV and HTLV-I. Human IL-15 is biologically active on mouse cells as measured by the dose-dependent stimulation of the proliferation of mouse CTLL cells. Recombinant Human IL-15 is a 12.9 kDa protein consisting of 115 amino acid residues.

Animal-Free Recombinant Human IL-15 (Legacy Tebubio ref. 167AF-15). IL-15 is an immunomodulating cytokine that stimulates the proliferation of T lymphocytes and shares many biological properties with IL-2. IL-15 exerts its biological activities primarily on T cells. It is also essential in the development, survival and activation of NK cells. Increased expression of IL-15 has been linked to rheumatoid arthritis, inflammatory bowel disease, and diseases affiliated with retroviruses HIV and HTLV-I. Human IL-15 is biologically active on mouse cells as measured by the dose-dependent stimulation of the proliferation of mouse CTLL cells. Recombinant Human IL-15 is a 12.9 kDa protein consisting of 115 amino acid residues.

Animal-Free Recombinant Human IL-16 (121 a.a.) (Legacy Tebubio ref. 167AF-16A). IL-16 is a CD8+ T cell-derived cytokine that induces chemotaxis of CD4+ T cells, CD4+ monocytes, and eosinophils. Analysis by gel filtration suggests that, under physiological conditions, hIL-16 exists predominantly as a noncovalently linked multimer, but that some IL-16 may exist as a monomer. However, only the multimeric form appears to possess chemotactic activity, suggesting that receptor cross-linking may be required for activity. IL-16 also induces expression of IL-2 receptor (IL-2R) and MHC class II molecules on CD4 + T cells. Human and murine IL-16 show significant cross-species reactivity. Recombinant Human IL-16 is a 12.4 kDa protein consisting of 121 amino acid residues.

Animal-Free Recombinant Human IL-16 (121 a.a.) (Legacy Tebubio ref. 167AF-16A). IL-16 is a CD8+ T cell-derived cytokine that induces chemotaxis of CD4+ T cells, CD4+ monocytes, and eosinophils. Analysis by gel filtration suggests that, under physiological conditions, hIL-16 exists predominantly as a noncovalently linked multimer, but that some IL-16 may exist as a monomer. However, only the multimeric form appears to possess chemotactic activity, suggesting that receptor cross-linking may be required for activity. IL-16 also induces expression of IL-2 receptor (IL-2R) and MHC class II molecules on CD4 + T cells. Human and murine IL-16 show significant cross-species reactivity. Recombinant Human IL-16 is a 12.4 kDa protein consisting of 121 amino acid residues.

Animal-Free Recombinant Human IL-17A (Legacy Tebubio ref. 167AF-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-17A (Legacy Tebubio ref. 167AF-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-19 (Legacy Tebubio ref. 167AF-19). IL-19 belongs to 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. Preliminary data suggests that IL-19 is a proinflammatory cytokine, because it up-regulates IL-6 and TNF-α, and induces apoptosis through TNF-α. IL-19 signals through the type I IL-20R. Human and murine IL-19 share 71% amino acid sequence identity. Recombinant Human IL-19 is a 35.8 kDa homodimer of two 154 amino acid chains. In solution, IL-19 exists predominantly as a non-disulfide-linked dimer.