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背景介绍 IL-10 is produced by mouse Th2-cells following their stimulation by lectins. The main source for B-cell derived IL-10 in mice are Ly1 B-cells that express CD5 (Ly1) and CD11. In humans IL-10 is produced by activated CD8(+) peripheral blood T-cells, by T-helper CD4(+) T-cell clones after both antigen-specific and polyclonal activation, by B- cell lymphomas, and by monocytes following cell activation by bacterial lipopolysaccharides and mast cells. IL-10 is a homodimeric protein with subunits having a length of 160 amino acids. Human Interleukin-10 shows 73% amino acid homology with mouse Interleukin-10. The murine IL-10 receptor has been cloned. This receptor is a protein of approximately 110 kDa that binds murine IL-10 specifically. This receptor is structurally related to receptors for IFN. The CD nomenclature for this receptor is CDw210. IL-10 inhibits the synthesis of a number of cytokines such as IFN-gamma, IL-2 and TNF-beta in Th1 T-helper subpopulations of T-cells but not of Th2 T-helper cells. This activity is antagonized by IL-4. The inhibitory effect on IFN- gamma production is indirect and appears to be the result of a suppression of IL-12 synthesis by accessory cells. In the human system, IL-10 is produced by, and down-regulates the function of Th1 and Th2 cells. 产品介绍 Recombinant Mouse IL-10 is a disulfide-linked monomer protein consisting of 161 amino acid residues, and migrates as an approximately 19 kDa protein under non-reducing and reducing conditions in SDS-PAGE. Optimized DNA sequence encoding mouse Interleukin-10 mature chain was expressed in E. coli.
询价背景介绍 IL-10 is produced by mouse Th2-cells following their stimulation by lectins. The main source for B-cell derived IL-10 in mice are Ly1 B-cells that express CD5 (Ly1) and CD11. In humans IL-10 is produced by activated CD8(+) peripheral blood T-cells, by T-helper CD4(+) T-cell clones after both antigen-specific and polyclonal activation, by B- cell lymphomas, and by monocytes following cell activation by bacterial lipopolysaccharides and mast cells. IL-10 is a homodimeric protein with subunits having a length of 160 amino acids. Human Interleukin-10 shows 73% amino acid homology with mouse Interleukin-10. The murine IL-10 receptor has been cloned. This receptor is a protein of approximately 110 kDa that binds murine IL-10 specifically. This receptor is structurally related to receptors for IFN. The CD nomenclature for this receptor is CDw210. IL-10 inhibits the synthesis of a number of cytokines such as IFN-gamma, IL-2 and TNF-beta in Th1 T-helper subpopulations of T-cells but not of Th2 T-helper cells. This activity is antagonized by IL-4. The inhibitory effect on IFN- gamma production is indirect and appears to be the result of a suppression of IL-12 synthesis by accessory cells. In the human system, IL-10 is produced by, and down-regulates the function of Th1 and Th2 cells. 产品介绍 Recombinant Human Interleukin-10 is a disulfide-linked monomer protein consisting of 161 amino acid residues, and migrates as an approximately 19 kDa protein under non-reducing and reducing conditions in SDS-PAGE. Optimized DNA sequence encoding human Interleukin-10 mature chain was expressed in E. coli.
询价背景介绍 IL-10 is produced by mouse Th2-cells following their stimulation by lectins. The main source for B-cell derived IL-10 in mice are Ly1 B-cells that express CD5 (Ly1) and CD11. In humans IL-10 is produced by activated CD8(+) peripheral blood T-cells, by T-helper CD4(+) T-cell clones after both antigen-specific and polyclonal activation, by B- cell lymphomas, and by monocytes following cell activation by bacterial lipopolysaccharides and mast cells. IL-10 is a homodimeric protein with subunits having a length of 160 amino acids. Human Interleukin-10 shows 73% amino acid homology with mouse Interleukin-10. The murine IL-10 receptor has been cloned. This receptor is a protein of approximately 110 kDa that binds murine IL-10 specifically. This receptor is structurally related to receptors for IFN. The CD nomenclature for this receptor is CDw210. IL-10 inhibits the synthesis of a number of cytokines such as IFN-gamma, IL-2 and TNF-beta in Th1 T-helper subpopulations of T-cells but not of Th2 T-helper cells. This activity is antagonized by IL-4. The inhibitory effect on IFN- gamma production is indirect and appears to be the result of a suppression of IL-12 synthesis by accessory cells. In the human system, IL-10 is produced by, and down-regulates the function of Th1 and Th2 cells. 产品介绍 Recombinant Human Interleukin-10 is a disulfide-linked monomer protein consisting of 161 amino acid residues, and migrates as an approximately 19 kDa protein under non-reducing and reducing conditions in SDS-PAGE. Optimized DNA sequence encoding human Interleukin-10 mature chain was expressed in E. coli.
询价背景介绍 Monocytes are the main source of secreted IL-1. They express predominantly IL-1beta while human keratinocytes express large amounts of IL-1alpha. Murine macrophages display a transition from IL-1beta to IL-1alpha production during maturation of monocytes into inflammatory macrophages.There are two functionally almost equivalent forms of IL-1, IL-1alpha and IL-1beta that are encoded by two different genes. IL1-beta is the predominant form in humans while it is IL-1alpha in mice. Both forms of IL-1 bind to the same receptor and therefore also show similar if not identical biological activities. The IL-1beta but not the IL-1alpha precursor must be processed before it can bind to the receptor. Both forms of IL-1 bind to the same receptor and therefore also show similar if not identical biological activities. The receptor isolated from T-cells is expressed predominantly on T-cells and cells of mesenchymal origin. It binds both types of IL-1 with equal affinity. This type is called also Type 1 receptor. It has been designated CD121a. The Type 2 receptor has been designated CD121b. It is isolated from B-cells, granulocytes, and macrophages. It is expressed predominantly on B-cells and cells of the myelomonocytic lineage and is encoded by a separate gene. 产品介绍 Recombinant IL-1 beta is a disulfide-linked monomer protein consisting of two 153 amino acid residues. Recombinant IL-1 beta migrates as an approximately 17 kDa protein under non-reducing conditions and reducing conditions in SDS-PAGE. Optimized DNA sequence encoding murine Interleukin-1 beta mature chain was expressed in E. coli.
询价背景介绍 Monocytes are the main source of secreted IL-1. They express predominantly IL-1beta while human keratinocytes express large amounts of IL-1alpha. Murine macrophages display a transition from IL-1beta to IL-1alpha production during maturation of monocytes into inflammatory macrophages.There are two functionally almost equivalent forms of IL-1, IL-1alpha and IL-1beta that are encoded by two different genes. IL1-beta is the predominant form in humans while it is IL-1alpha in mice. Both forms of IL-1 bind to the same receptor and therefore also show similar if not identical biological activities. The IL-1beta but not the IL-1alpha precursor must be processed before it can bind to the receptor. Both forms of IL-1 bind to the same receptor and therefore also show similar if not identical biological activities. The receptor isolated from T-cells is expressed predominantly on T-cells and cells of mesenchymal origin. It binds both types of IL-1 with equal affinity. This type is called also Type 1 receptor. It has been designated CD121a. The Type 2 receptor has been designated CD121b. It is isolated from B-cells, granulocytes, and macrophages. It is expressed predominantly on B-cells and cells of the myelomonocytic lineage and is encoded by a separate gene. 产品介绍 Recombinant IL-1 beta is a disulfide-linked monomer protein consisting of two 153 amino acid residues. Recombinant IL-1 beta migrates as an approximately 17 kDa protein under non-reducing conditions and reducing conditions in SDS-PAGE. Optimized DNA sequence encoding murine Interleukin-1 beta mature chain was expressed in E. coli.
询价背景介绍 Monocytes are the main source of secreted IL-1. They express predominantly IL-1beta while human keratinocytes express large amounts of IL-1alpha. Murine macrophages display a transition from IL-1beta to IL-1alpha production during maturation of monocytes into inflammatory macrophages.There are two functionally almost equivalent forms of IL-1, IL-1alpha and IL-1beta that are encoded by two different genes. IL1-beta is the predominant form in humans while it is IL-1alpha in mice. Both forms of IL-1 bind to the same receptor and therefore also show similar if not identical biological activities. The IL-1beta but not the IL-1alpha precursor must be processed before it can bind to the receptor. Both forms of IL-1 bind to the same receptor and therefore also show similar if not identical biological activities. The receptor isolated from T-cells is expressed predominantly on T-cells and cells of mesenchymal origin. It binds both types of IL-1 with equal affinity. This type is called also Type 1 receptor. It has been designated CD121a. The Type 2 receptor has been designated CD121b. It is isolated from B-cells, granulocytes, and macrophages. It is expressed predominantly on B-cells and cells of the myelomonocytic lineage and is encoded by a separate gene. 产品介绍 Recombinant IL-1a is a disulfide-linked monomer protein consisting of 157 amino acid residues and migrates as an approximately 18 kDa protein under non-reducing conditions and reducing conditions in SDS-PAGE. Optimized DNA sequence encoding murine Interleukin-1 alpha mature chain was expressed in E. coli.
询价背景介绍 Monocytes are the main source of secreted IL-1. They express predominantly IL-1beta while human keratinocytes express large amounts of IL-1alpha. Murine macrophages display a transition from IL-1beta to IL-1alpha production during maturation of monocytes into inflammatory macrophages.There are two functionally almost equivalent forms of IL-1, IL-1alpha and IL-1beta that are encoded by two different genes. IL1-beta is the predominant form in humans while it is IL-1alpha in mice. Both forms of IL-1 bind to the same receptor and therefore also show similar if not identical biological activities. The IL-1beta but not the IL-1alpha precursor must be processed before it can bind to the receptor. Both forms of IL-1 bind to the same receptor and therefore also show similar if not identical biological activities. The receptor isolated from T-cells is expressed predominantly on T-cells and cells of mesenchymal origin. It binds both types of IL-1 with equal affinity. This type is called also Type 1 receptor. It has been designated CD121a. The Type 2 receptor has been designated CD121b. It is isolated from B-cells, granulocytes, and macrophages. It is expressed predominantly on B-cells and cells of the myelomonocytic lineage and is encoded by a separate gene. 产品介绍 Recombinant IL-1a is a disulfide-linked monomer protein consisting of 157 amino acid residues and migrates as an approximately 18 kDa protein under non-reducing conditions and reducing conditions in SDS-PAGE. Optimized DNA sequence encoding murine Interleukin-1 alpha mature chain was expressed in E. coli.
询价背景介绍 IL1ra is found in the conditioned medium of a variety of cells and is produced by macrophages, monocytes,neutrophils. The soluble form of IL1ra has been shown to be produced by hepatocytes, and to be regulated by pro- inflammatory cytokines. 产品介绍 Recombinant IL-1RA is a disulfide-linked monomer protein consisting of 153 amino acid residues, and migrates as an approximately 17 kDa protein under non-reducing and reducing conditions in SDS-PAGE. Optimized DNA sequence encoding Human interleukin-1 receptor antagonist mature chain was expressed in E. coli.
询价背景介绍 IL1ra is found in the conditioned medium of a variety of cells and is produced by macrophages, monocytes,neutrophils. The soluble form of IL1ra has been shown to be produced by hepatocytes, and to be regulated by pro- inflammatory cytokines. 产品介绍 Recombinant IL-1RA is a disulfide-linked monomer protein consisting of 153 amino acid residues, and migrates as an approximately 17 kDa protein under non-reducing and reducing conditions in SDS-PAGE. Optimized DNA sequence encoding Human interleukin-1 receptor antagonist mature chain was expressed in E. coli.
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