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背景介绍
IP10 shows homology to PF4 (platelet factor-4) and belongs to the family of chemotactic cytokines known as Chemokines. The receptor for IP-10 is CXCR3. IP-10 has been shown to bind to the virus-encoded viroceptor M3. The expression of IP-10 from a variety of cells, including monocytes, endothelial cells, keratinocytes, and fibroblasts, is induced by IFN-gamma and TNF-alpha. Human neutrophils produce IP-10 in response to IFN- gamma in combination with either TNF-alpha or bacterial lipopolysaccharides. IP-10 probably also plays a role in regulation of the growth of immature hematopoietic progenitor cells. It has been shown to suppress in vitro colony formation of highly enriched cells expressing the cell surface marker CD34 in the presence of SCF, GM-CSF, or SCF and EPO, but not in their absence with the exception of SCF.
Native human IP-10/CXCL10, generated by the proteolytic removal of the signal peptide and propeptide, the molecule has a calculated molecular mass of approximately 9 kDa.
产品介绍
Recombinant human IP-10 (also known as CXCL10) is a disulfide-linked homodimeric protein consisting of 78 amino acid residues, and migrates as an approximately 9 kDa protein under non-reducing and reducing conditions in SDS-PAGE. Optimized DNA sequence encoding Human IP-10 mature chain was expressed in E. coli.
背景介绍 Native human Insulin is generated by the proteolytic removal of the signal peptide and propeptide, and has a calculated molecular mass of approximately 6 kDa 产品介绍 Recombinant human Insulin is a disulfide-linked homodimeric protein consisting of 51 amino acid residues, and migrates as an approximately 6 kDa protein under non-reducing conditions and reducing conditions in SDS-PAGE. Optimized DNA sequence encoding Human Insulin mature chain was expressed in E. coli.
询价背景介绍 Native human Insulin is generated by the proteolytic removal of the signal peptide and propeptide, and has a calculated molecular mass of approximately 6 kDa 产品介绍 Recombinant human Insulin is a disulfide-linked homodimeric protein consisting of 51 amino acid residues, and migrates as an approximately 6 kDa protein under non-reducing conditions and reducing conditions in SDS-PAGE. Optimized DNA sequence encoding Human Insulin mature chain was expressed in E. coli.
询价背景介绍 IL-8 is produced by stimulated monocytes but not by tissue macrophages or T-lymphocytes. In many cell types the synthesis of IL-8 is strongly stimulated by IL-1 and TNF-alpha. In human skin fibroblasts, the expression of IL-8 is enhanced by Leukoregulin.The expression of IL-8 from resting and stimulated human blood monocytes is up-regulated by IL-7. In chondrocytes, the synthesis of IL-8 is stimulated by IL1-beta TNF-alpha and bacterial lipopolysaccharides. In human astrocytes, the synthesis and secretion of IL-8 is induced by IL-1 and TNF-alpha. The IL-8 receptor (CD128) is a dimeric glycoprotein consisting of a 59 kDa and a 67 kDa subunit. It is expressed in many different cell types including those not responding to IL-8. The biological activities of IL-8 resemble those of a related protein, NAP-2. IL-8 differs from all other cytokines in its ability to specifically activate neutrophil granulocytes. In neutrophils, IL-8 causes a transient increase in cytosolic calcium levels and the release of enzymes from granules. IL-8 also enhances the metabolism of reactive oxygen species and increases chemotaxis and the enhanced expression of adhesion molecules. Pre-activation by IL-3 is required to render basophils and neutrophils susceptible to further activation by IL-8. Native human IL-8, generated by the proteolytic removal of the signal peptide and propeptide, has a calculated molecular mass of approximately 8 kDa. 产品介绍 Recombinant human Interleukin-8 is a disulfide-linked monomer protein consisting of 73 amino acid residues, migrates as an approximately 8 kDa protein under non-reducing and reducing conditions in SDS-PAGE. Optimized DNA sequence encoding Human Interleukin-8 mature chain was expressed in E. coli.
询价背景介绍 IL-8 is produced by stimulated monocytes but not by tissue macrophages or T-lymphocytes. In many cell types the synthesis of IL-8 is strongly stimulated by IL-1 and TNF-alpha. In human skin fibroblasts, the expression of IL-8 is enhanced by Leukoregulin.The expression of IL-8 from resting and stimulated human blood monocytes is up-regulated by IL-7. In chondrocytes, the synthesis of IL-8 is stimulated by IL1-beta TNF-alpha and bacterial lipopolysaccharides. In human astrocytes, the synthesis and secretion of IL-8 is induced by IL-1 and TNF-alpha. The IL-8 receptor (CD128) is a dimeric glycoprotein consisting of a 59 kDa and a 67 kDa subunit. It is expressed in many different cell types including those not responding to IL-8. The biological activities of IL-8 resemble those of a related protein, NAP-2. IL-8 differs from all other cytokines in its ability to specifically activate neutrophil granulocytes. In neutrophils, IL-8 causes a transient increase in cytosolic calcium levels and the release of enzymes from granules. IL-8 also enhances the metabolism of reactive oxygen species and increases chemotaxis and the enhanced expression of adhesion molecules. Pre-activation by IL-3 is required to render basophils and neutrophils susceptible to further activation by IL-8. Native human IL-8, generated by the proteolytic removal of the signal peptide and propeptide, has a calculated molecular mass of approximately 8 kDa. 产品介绍 Recombinant human Interleukin-8 is a disulfide-linked monomer protein consisting of 73 amino acid residues, migrates as an approximately 8 kDa protein under non-reducing and reducing conditions in SDS-PAGE. Optimized DNA sequence encoding Human Interleukin-8 mature chain was expressed in E. coli.
询价背景介绍 IL-7 is secreted constitutively into the conditioned medium of adherent bone marrow stromal cells and thymic cells. Mouse and human keratinocytes have been shown also to express and secrete IL-7. Human (152 amino acids) and murine IL-7 (129 amino acids) show 60% sequence homology at the protein level. The human IL-7 receptor, designated CD127, is an integral strongly glycosylated membrane protein of 76 kDa expressed on activated T-cells. IL-7 receptors are expressed on pre-B-cells and their progenitors and bone marrow macrophages, but they are not expressed on mature B-cells. Functional IL-7 receptors are also found on the cell surface of multiphenotypic, biphenotypic, and immature lymphoid progenitors of B-cells with the gene arrangement of the heavy immunoglobulin chain such as those observed in the germ line. 产品介绍 Recombinant human IL-7 is a disulfide-linked monomeric protein consisting of 153 amino acid residues, and migrates as an approximately 17 kDa protein under non-reducing conditions and reducing conditions in SDS-PAGE. Optimized DNA sequence encoding Human Interleukin-7 mature chain was expressed in E. coli.
询价背景介绍 IL-7 is secreted constitutively into the conditioned medium of adherent bone marrow stromal cells and thymic cells. Mouse and human keratinocytes have been shown also to express and secrete IL-7. Human (152 amino acids) and murine IL-7 (129 amino acids) show 60% sequence homology at the protein level. The human IL-7 receptor, designated CD127, is an integral strongly glycosylated membrane protein of 76 kDa expressed on activated T-cells. IL-7 receptors are expressed on pre-B-cells and their progenitors and bone marrow macrophages, but they are not expressed on mature B-cells. Functional IL-7 receptors are also found on the cell surface of multiphenotypic, biphenotypic, and immature lymphoid progenitors of B-cells with the gene arrangement of the heavy immunoglobulin chain such as those observed in the germ line. 产品介绍 Recombinant human IL-7 is a disulfide-linked monomeric protein consisting of 153 amino acid residues, and migrates as an approximately 17 kDa protein under non-reducing conditions and reducing conditions in SDS-PAGE. Optimized DNA sequence encoding Human Interleukin-7 mature chain was expressed in E. coli.
询价背景介绍 IL-6 is a member of a family of cytokines, which also includes LIF, CNTF, Oncostatin M, IL11, and CT- 1. All known members of the IL-6 cytokine family induce hepatic expression of acute phase proteins. IL-6 is produced by many different cell types. The main sources in vivo are stimulated monocytes, fibroblasts, and endothelial cells. Macrophages, T-cells and B-lymphocytes, granulocytes, smooth muscle cells, eosinophils, chondrocytes, osteoblasts, mast cells, glial cells, and keratinocytes also produce IL-6 after stimulation. The IL-6 receptor is expressed on T-cells, mitogen-activated B-cells, peripheral monocytes and some macrophage- and B-cell derived tumor cell types. It is not expressed in resting B-cells but in resting T-cells. The IL-6 receptor (CD126) is a strongly glycosylated protein of 80 kDa and a length of 449 amino acids. 产品介绍 Recombinant murine IL-6 is a disulfide-linked homodimeric protein consisting of 188 amino acid residues, and migrates as an approximately 22 kDa protein under non-reducing and reducing conditions in SDS-PAGE. Optimized DNA sequence encoding mouse Interleukin-6 mature chain was expressed in E. coli.
询价背景介绍 IL-6 is a member of a family of cytokines, which also includes LIF, CNTF, Oncostatin M, IL11, and CT- 1. All known members of the IL-6 cytokine family induce hepatic expression of acute phase proteins. IL-6 is produced by many different cell types. The main sources in vivo are stimulated monocytes, fibroblasts, and endothelial cells. Macrophages, T-cells and B-lymphocytes, granulocytes, smooth muscle cells, eosinophils, chondrocytes, osteoblasts, mast cells, glial cells, and keratinocytes also produce IL-6 after stimulation. The IL-6 receptor is expressed on T-cells, mitogen-activated B-cells, peripheral monocytes and some macrophage- and B-cell derived tumor cell types. It is not expressed in resting B-cells but in resting T-cells. The IL-6 receptor (CD126) is a strongly glycosylated protein of 80 kDa and a length of 449 amino acids. 产品介绍 Recombinant murine IL-6 is a disulfide-linked homodimeric protein consisting of 188 amino acid residues, and migrates as an approximately 22 kDa protein under non-reducing and reducing conditions in SDS-PAGE. Optimized DNA sequence encoding mouse Interleukin-6 mature chain was expressed in E. coli.
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