Results for Other Proteins ( 58180 )
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Animal-Free Recombinant Murine IL-2 (Legacy Tebubio ref. 167AF-212-12). IL-2 is a powerful immunoregulatory lymphokine produced by T-cells in response to antigenic or mitogenic stimulation. IL-2/IL-2R signaling is required for T-cell proliferation and other fundamental functions that are essential for the immune response. IL-2 stimulates growth and differentiation of B-cells, NK cells, lymphokine-activated killer cells, monocytes, macrophages and oligodendrocytes. Recombinant Murine IL-2 is a 17.2 kDa protein containing 148 amino acid residues.
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Animal-Free Recombinant Murine SCF (Legacy Tebubio ref. 167AF-250-03). SCF is a hematopoietic growth factor that exerts its activity by signaling through the c-Kit receptor. SCF and c-Kit are essential for the survival, proliferation and differentiation of hematopoietic cells committed to the melanocyte and germ cell lineages. Human SCF manifests low activity on murine cells, while murine and rat SCF are fully active on human cells. The human SCF gene encodes for a 273 amino acid transmembrane protein, which contains a 25 amino acid N-terminal signal sequence, a 189 amino acid extracellular domain, a 23 amino acid transmembrane domain, and a 36 amino acid cytoplasmic domain. The secreted soluble form of SCF is generated by proteolytic processing of the membrane anchored precursor. Recombinant Murine SCF is an 18.3 kDa polypeptide containing 165 amino acid residues, which corresponds to the sequence of the secreted soluble form of SCF.
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Animal-Free Recombinant Murine Noggin (Legacy Tebubio ref. 167AF-250-38). Noggin belongs to a group of diffusible proteins that bind to ligands of the TGF-beta family, and regulate their activity by inhibiting their access to signaling receptors. Noggin was originally identified as a BMP-4 antagonist whose action was critical for proper formation of the head and other dorsal structures. Consequently, noggin has been shown to modulate the activities of other BMPs including BMP-2,-7,-13, and -14. Targeted deletion of noggin in mice results in prenatal death, and a recessive phenotype displaying a severely malformed skeletal system. Conversely, transgenic mice over-expressing noggin in mature osteoblasts display impaired osteoblastic differentiation, reduced bone formation, and severe osteoporosis. Recombinant Murine Noggin is a 46.4 kDa disulfide-linked homodimer consisting of two 206 amino acid polypeptide chains.
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Animal-Free Recombinant Murine Noggin (Legacy Tebubio ref. 167AF-250-38). Noggin belongs to a group of diffusible proteins that bind to ligands of the TGF-beta family, and regulate their activity by inhibiting their access to signaling receptors. Noggin was originally identified as a BMP-4 antagonist whose action was critical for proper formation of the head and other dorsal structures. Consequently, noggin has been shown to modulate the activities of other BMPs including BMP-2,-7,-13, and -14. Targeted deletion of noggin in mice results in prenatal death, and a recessive phenotype displaying a severely malformed skeletal system. Conversely, transgenic mice over-expressing noggin in mature osteoblasts display impaired osteoblastic differentiation, reduced bone formation, and severe osteoporosis. Recombinant Murine Noggin is a 46.4 kDa disulfide-linked homodimer consisting of two 206 amino acid polypeptide chains.
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Animal-Free Recombinant Human IFN-gamma (Legacy Tebubio ref. 167AF-300-02). 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 Human IFN-gamma is a 16.8 kDa protein containing 144 amino acid residues.
- From: €102.00
Animal-Free Recombinant Human IFN-gamma (Legacy Tebubio ref. 167AF-300-02). 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 Human IFN-gamma is a 16.8 kDa protein containing 144 amino acid residues.
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Animal-Free Recombinant Human IFN-beta (Legacy Tebubio ref. 167AF-300-02B). Proteins of this family play an important role in inducing non-specific resistance against a broad range of viral infections. They also affect cell proliferation and modulate immune responses. Produced by peripheral blood leukocytes and lymphoblastoid cells, IFN-alpha is an acid-stable molecule that signals through IFN-alpha/betaR, which is also used by IFN-beta. Both IFNs have similar anti-viral activity and regulate expression of MHC class I antigens. IFN-alpha contains four highly conserved cysteine residues that form two disulfide bonds, one of which is necessary for biological activity. PeproTech's Recombinant Human IFN-beta is a 20.0 kDa protein containing 166 amino acid residues.
- From: €103.00
Animal-Free Recombinant Human IFN-beta (Legacy Tebubio ref. 167AF-300-02B). Proteins of this family play an important role in inducing non-specific resistance against a broad range of viral infections. They also affect cell proliferation and modulate immune responses. Produced by peripheral blood leukocytes and lymphoblastoid cells, IFN-alpha is an acid-stable molecule that signals through IFN-alpha/betaR, which is also used by IFN-beta. Both IFNs have similar anti-viral activity and regulate expression of MHC class I antigens. IFN-alpha contains four highly conserved cysteine residues that form two disulfide bonds, one of which is necessary for biological activity. PeproTech's Recombinant Human IFN-beta is a 20.0 kDa protein containing 166 amino acid residues.
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Animal-Free Recombinant Human IFN-lambda1 (Legacy Tebubio ref. 167AF-300-02L). IFN lambda1, 2, and 3 (also known as IL-29, IL-28A and IL-28B respectively) are distantly related to the IL-10 family and the interferons. All three IFN-lambdas use a distinct receptor system composed of an IFN-lambdaR1 subunit (also called CRF2-12) and IL-10R2 subunit (also called CRF2-14). Signaling through this receptor system induces antiviral defenses similar to, but distinct from, that of type I interferons. Recombinant Human IFN-lambda1 is a 19.8 kDa protein containing 178 amino acid residues.