Cytokines & Chemokines

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-17D (Legacy Tebubio ref. 167AF-200-27). IL-17D is a disulfide-linked homodimer of two 185 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-17D has the ability to stimulate the production of IL-6, IL-8 and GM-CSF, and inhibits hemopoiesis of myeloid progenitor cells in colony-forming assays. Recombinant Human IL-17D is a 40.5 kDa disulfide-linked homodimer of two 185 amino acid polypeptide chains.

Animal-Free Recombinant Human IL-17D (Legacy Tebubio ref. 167AF-200-27). IL-17D is a disulfide-linked homodimer of two 185 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-17D has the ability to stimulate the production of IL-6, IL-8 and GM-CSF, and inhibits hemopoiesis of myeloid progenitor cells in colony-forming assays. Recombinant Human IL-17D is a 40.5 kDa disulfide-linked homodimer of two 185 amino acid polypeptide chains.

Animal-Free Recombinant Human IL-33 (Legacy Tebubio ref. 167AF-200-33). Human IL-33 is a proinflammatory protein that shares structural and functional characteristics with the IL-1 cytokine family. It binds and signals through the IL-1RL1/ST2 receptor, to activate NF-kappaB and MAP kinases. IL-33 induces production of TH2 cell related cytokines, including IL-4, IL-5 and IL-13, and exerts multiple inflammation related bioactivities. Recombinant Human IL-33 is a 17.9 kDa protein containing 159 amino acid residues.

Animal-Free Recombinant Human IL-33 (Legacy Tebubio ref. 167AF-200-33). Human IL-33 is a proinflammatory protein that shares structural and functional characteristics with the IL-1 cytokine family. It binds and signals through the IL-1RL1/ST2 receptor, to activate NF-kappaB and MAP kinases. IL-33 induces production of TH2 cell related cytokines, including IL-4, IL-5 and IL-13, and exerts multiple inflammation related bioactivities. Recombinant Human IL-33 is a 17.9 kDa protein containing 159 amino acid residues.

Animal-Free Recombinant Human IL-37 (IL-1F7) (Legacy Tebubio ref. 167AF-200-39). The IL-1 family is comprised of 11 structurally related ligands, including recently re-named IL-37 (IL-1F7), which acts as a modulator of the immune response. Reduction of IL-37 synthesis in PBMCs leads to increased production of proinflammatory cytokines including IL-1 alpha, IL-1beta, IL-6 and TNF- alpha. The role of IL-37 as an inhibitor of the innate inflammatory response is also corroborated by the observation that it is highly expressed in synovial tissue from patients with rheumatoid arthritis. Full length IL-37 resides primarily in the cytoplasm, but after activation through cleavage by CASP1, it can translocate to the nucleus where it exerts its activity by direct interaction with SMAD3. Recombinant Human IL-37 is a 19.4 kDa protein consisting of 174 amino acids, corresponding to the mature activated form of IL-37.

Animal-Free Recombinant Human IL-37 (IL-1F7) (Legacy Tebubio ref. 167AF-200-39). The IL-1 family is comprised of 11 structurally related ligands, including recently re-named IL-37 (IL-1F7), which acts as a modulator of the immune response. Reduction of IL-37 synthesis in PBMCs leads to increased production of proinflammatory cytokines including IL-1 alpha, IL-1beta, IL-6 and TNF- alpha. The role of IL-37 as an inhibitor of the innate inflammatory response is also corroborated by the observation that it is highly expressed in synovial tissue from patients with rheumatoid arthritis. Full length IL-37 resides primarily in the cytoplasm, but after activation through cleavage by CASP1, it can translocate to the nucleus where it exerts its activity by direct interaction with SMAD3. Recombinant Human IL-37 is a 19.4 kDa protein consisting of 174 amino acids, corresponding to the mature activated form of IL-37.

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.