Other Proteins

Animal-Free Recombinant Murine IFN-gamma (Legacy Tebubio ref. 167AF-315-05). IFN-gamma is an acid-labile interferon produced by CD4 and CD8 T lymphocytes, as well as activated NK cells. IFN-gamma receptors are present in most immune cells, which respond to IFN-gamma signaling by increasing the surface expression of class I MHC proteins. This promotes the presentation of antigen to T-helper (CD4+) cells. IFN-gamma signaling in antigen-presenting, cells and antigen-recognizing B and T lymphocytes, regulates the antigen-specific phases of the immune response. Additionally, IFN-gamma stimulates a number of lymphoid cell functions, including the anti-microbial and anti-tumor responses of macrophages, NK cells, and neutrophils. Human IFN-gamma is species-specific and is biologically active only in human and primate cells. Recombinant Murine IFN-gamma is a 15.6 kDa protein containing 134 amino acid residues.

Animal-Free Recombinant Murine EGF (Legacy Tebubio ref. 167AF-315-09). EGF is a potent growth factor that stimulates the proliferation of various epidermal and epithelial cells. Additionally, EGF has been shown to inhibit gastric secretion, and to be involved in wound healing. EGF signals through a receptor known as c-erbB, which is a class I tyrosine kinase receptor. This receptor also binds with TGF-alpha and VGF (vaccinia virus growth factor). Recombinant Murine EGF is a 6.0 kDa globular protein containing 53 amino acid residues, including 3 intramolecular disulfide bonds.

Animal-Free Recombinant Murine EGF (Legacy Tebubio ref. 167AF-315-09). EGF is a potent growth factor that stimulates the proliferation of various epidermal and epithelial cells. Additionally, EGF has been shown to inhibit gastric secretion, and to be involved in wound healing. EGF signals through a receptor known as c-erbB, which is a class I tyrosine kinase receptor. This receptor also binds with TGF-alpha and VGF (vaccinia virus growth factor). Recombinant Murine EGF is a 6.0 kDa globular protein containing 53 amino acid residues, including 3 intramolecular disulfide bonds.

Animal-Free Recombinant Murine LIGHT (Legacy Tebubio ref. 167AF-315-12). LIGHT belongs to the TNF family of ligands, and can signal through the herpes virus entry mediator type A receptor (HVEM, TNFRSF14), LTbetaR, or bind to a decoy receptor, DcR3. It is expressed in splenocytes, activated PBL, CD8+ tumor infiltrating lymphocytes, granulocytes, and monocytes. LIGHT has the ability to activate NF-kappaB, to co-stimulate the activation of lymphocytes and to induce apoptosis in certain human tumor cells. Recombinant Murine LIGHT is a 20.1 kDa protein containing 183 amino acid residues, comprising the TNF-homologous region of the LIGHT extracellular domain.

Animal-Free Recombinant Murine LIGHT (Legacy Tebubio ref. 167AF-315-12). LIGHT belongs to the TNF family of ligands, and can signal through the herpes virus entry mediator type A receptor (HVEM, TNFRSF14), LTbetaR, or bind to a decoy receptor, DcR3. It is expressed in splenocytes, activated PBL, CD8+ tumor infiltrating lymphocytes, granulocytes, and monocytes. LIGHT has the ability to activate NF-kappaB, to co-stimulate the activation of lymphocytes and to induce apoptosis in certain human tumor cells. Recombinant Murine LIGHT is a 20.1 kDa protein containing 183 amino acid residues, comprising the TNF-homologous region of the LIGHT extracellular domain.

Animal-Free Recombinant Murine TPO (Legacy Tebubio ref. 167AF-315-14). TPO is a lineage-specific growth factor produced in the liver, kidney and skeletal muscle. It stimulates the proliferation and maturation of megakaryocytes, and promotes increased circulating levels of platelets in vivo. TPO signals through the c-mpl receptor, and acts as an important regulator of circulating platelets. Human and murine TPO exhibit cross-species reactivity. Recombinant Murine TPO is a fully biologically active 174 amino acid polypeptide (18.7 kDa), which contains the erythropoietin-like domain of the full length TPO protein.

Animal-Free Recombinant Murine TPO (Legacy Tebubio ref. 167AF-315-14). TPO is a lineage-specific growth factor produced in the liver, kidney and skeletal muscle. It stimulates the proliferation and maturation of megakaryocytes, and promotes increased circulating levels of platelets in vivo. TPO signals through the c-mpl receptor, and acts as an important regulator of circulating platelets. Human and murine TPO exhibit cross-species reactivity. Recombinant Murine TPO is a fully biologically active 174 amino acid polypeptide (18.7 kDa), which contains the erythropoietin-like domain of the full length TPO protein.

Animal-Free Recombinant Human IGF-BP7 (Legacy Tebubio ref. 167AF-350-09). IGF-BPs control the distribution, function and activity of IGFs in various cell tissues and body fluids. Currently, there are seven named IGF-BPs that form high affinity complexes with both IGF-I and IGF-II. IGF-BP7 is expressed in a wide range of normal human tissues, and it generally shows reduced expression in cancer cell lines of prostate, breast, colon, and lung origin. It plays a role in skeletal myogenesis by binding to IGF in a manner that inhibits IGF-induced differentiation of skeletal myoblasts, without affecting IGF-induced proliferation. Additionally, IGF-BP7 suppresses growth and colony formation of prostate and breast cancer cell lines through an IGF-independent mechanism, which causes a delay in the G1 phase of the cell cycle and increased apoptosis. Recombinant Human IGF-BP7 is a 26.4 kDa protein consisting of 256 amino acid residues.

Animal-Free Recombinant Human IGF-BP7 (Legacy Tebubio ref. 167AF-350-09). IGF-BPs control the distribution, function and activity of IGFs in various cell tissues and body fluids. Currently, there are seven named IGF-BPs that form high affinity complexes with both IGF-I and IGF-II. IGF-BP7 is expressed in a wide range of normal human tissues, and it generally shows reduced expression in cancer cell lines of prostate, breast, colon, and lung origin. It plays a role in skeletal myogenesis by binding to IGF in a manner that inhibits IGF-induced differentiation of skeletal myoblasts, without affecting IGF-induced proliferation. Additionally, IGF-BP7 suppresses growth and colony formation of prostate and breast cancer cell lines through an IGF-independent mechanism, which causes a delay in the G1 phase of the cell cycle and increased apoptosis. Recombinant Human IGF-BP7 is a 26.4 kDa protein consisting of 256 amino acid residues.