Cytokines & Chemokines

Animal-Free Recombinant Human IL-11 (Legacy Tebubio ref. 167AF-200-11). IL-11 is a multifunctional cytokine produced by stromal cells, such as fibroblasts, epithelial cells and osteoclasts. It is expressed in a wide variety of tissues, including thymus, lung, bone, connective tissue and central nervous system. IL-11 plays an important regulatory role in hematopoiesis by stimulating growth of myeloid, erythroid and megakaryocyte progenitor cells. It also regulates bone metabolism, inhibits production of proinflammatory cytokines, and protects against gastromucosal injury. Recombinant Human IL-11 is a 19.3 kDa protein consisting of 179 amino acid residues.

Animal-Free Recombinant Human IL-11 (Legacy Tebubio ref. 167AF-200-11). IL-11 is a multifunctional cytokine produced by stromal cells, such as fibroblasts, epithelial cells and osteoclasts. It is expressed in a wide variety of tissues, including thymus, lung, bone, connective tissue and central nervous system. IL-11 plays an important regulatory role in hematopoiesis by stimulating growth of myeloid, erythroid and megakaryocyte progenitor cells. It also regulates bone metabolism, inhibits production of proinflammatory cytokines, and protects against gastromucosal injury. Recombinant Human IL-11 is a 19.3 kDa protein consisting of 179 amino acid residues.

Animal-Free Recombinant Human IL-13 (Legacy Tebubio ref. 167AF-200-13). 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-200-13). 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-200-15). 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-200-15). 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-200-16A). 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-200-16A). 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-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.