Results for Cytokines & Chemokines ( 1790 )
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Fractalkine, also named neurotactin, is a novel chemokine recently identified through bioinformatics. Fractalkine has a unique C-X3-C cysteine motif near the amino-terminus and is the first member of a fourth branch of the chemokine superfamily. Unlike other known chemokines, fractalkine is a type 1 membrane protein containing a chemokine domain tethered on a long mucin-like stalk. Human fractalkine cDNA encodes a 397 amino acid (aa) residue membrane protein with a 24 aa residue predicted signal peptide, a 76 aa residue chemokine domain, a 241 aa residue stalk region containing 17 degenerate mucin-like repeats, a 19 aa residue transmembrane segment and a 37 aa residue cytoplasmic domain. The extracellular domain of human fractalkine can be released, possibly by proteolysis at the dibasic cleavage site proximal to the membrane, to generate soluble fractalkine. The soluble chemokine domain of human fractalkine was reported to be chemotactic for T cells and monocytes while the soluble che
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Fractalkine, also named neurotactin, is a novel chemokine recently identified through bioinformatics. Fractalkine has a unique C-X3-C cysteine motif near the amino-terminus and is the first member of a fourth branch of the chemokine superfamily. Unlike other known chemokines, fractalkine is a type 1 membrane protein containing a chemokine domain tethered on a long mucin-like stalk. Human fractalkine cDNA encodes a 397 amino acid (aa) residue membrane protein with a 24 aa residue predicted signal peptide, a 76 aa residue chemokine domain, a 241 aa residue stalk region containing 17 degenerate mucin-like repeats, a 19 aa residue transmembrane segment and a 37 aa residue cytoplasmic domain. The extracellular domain of human fractalkine can be released, possibly by proteolysis at the dibasic cleavage site proximal to the membrane, to generate soluble fractalkine. The soluble chemokine domain of human fractalkine was reported to be chemotactic for T cells and monocytes while the soluble che
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CCL5 or RANTES (acronym for Regulated upon Activation, Normal T cell Expressed and presumably Secreted), was initially discovered by subtractive hybridization as a transcript expressed in T cells but not B cells. Eosinophilchemotactic activities released by thrombinstimulated human platelets have also been purified and found to be identical to RANTES. Besides T cells and platelets, RANTES has been reported to be produced by renal tubular epithelium, synovial fibroblasts and selected tumor cells.
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CCL5 or RANTES (acronym for Regulated upon Activation, Normal T cell Expressed and presumably Secreted), was initially discovered by subtractive hybridization as a transcript expressed in T cells but not B cells. Eosinophilchemotactic activities released by thrombinstimulated human platelets have also been purified and found to be identical to RANTES. Besides T cells and platelets, RANTES has been reported to be produced by renal tubular epithelium, synovial fibroblasts and selected tumor cells.
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CCL11 is a potent eosinophil chemoattractant that was originally purified from bronchoalveolar lavage fluid of guinea pigs sensitized by aerosol challenge with ovalbumin. Human CCL11 cDNA encodes a 97 amino acid residue precursor protein from which the aminoterminal 23 amino acid residues are cleaved to generate the 74 amino acid residue mature human CCL11. At the protein sequence level, mature human CCL11 is approximately 60% identical to mature mouse and guinea pig CCL11. Human CCL11 is chemotactic for eosinophils, but not mononuclear cells or neutrophils. The CC chemokine receptor 3 (CCR3) has now been identified to be a specific human CCL11 receptor. CCR3 has also been shown to serve as a cofactor for a restricted subset of primary HIV viruses and binding of CCL11 to CCR3 inhibited infection by the HIV isolates.
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CCL11 is a potent eosinophil chemoattractant that was originally purified from bronchoalveolar lavage fluid of guinea pigs sensitized by aerosol challenge with ovalbumin. Human CCL11 cDNA encodes a 97 amino acid residue precursor protein from which the aminoterminal 23 amino acid residues are cleaved to generate the 74 amino acid residue mature human CCL11. At the protein sequence level, mature human CCL11 is approximately 60% identical to mature mouse and guinea pig CCL11. Human CCL11 is chemotactic for eosinophils, but not mononuclear cells or neutrophils. The CC chemokine receptor 3 (CCR3) has now been identified to be a specific human CCL11 receptor. CCR3 has also been shown to serve as a cofactor for a restricted subset of primary HIV viruses and binding of CCL11 to CCR3 inhibited infection by the HIV isolates.
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CCL17 is a novel CC chemokine recently identified using a signal sequence trap method. CCL17 cDNA encodes a highly basic 94 amino acid residue precursor protein with a 23 aa residue signal peptide that is cleaved to generate the 71 aa residue mature secreted protein. Among CC chemokine family members, CCL17 has approximately 24 - 29% amino acid sequence identity with RANTES, MIP-1α, MIP-1β, MCP-1, MCP-2, MCP-3 and I-309. The gene for human CCL17 has been mapped to chromosome 16q13 rather than chromosome 17 where the genes for many human CC chemokines are clustered. CCL17 is constitutively expressed in thymus, and at a lower level in lung, colon, and small intestine. CCL17 is also transiently expressed in stimulated peripheral blood mononuclear cells.
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CCL17 is a novel CC chemokine recently identified using a signal sequence trap method. CCL17 cDNA encodes a highly basic 94 amino acid residue precursor protein with a 23 aa residue signal peptide that is cleaved to generate the 71 aa residue mature secreted protein. Among CC chemokine family members, CCL17 has approximately 24 - 29% amino acid sequence identity with RANTES, MIP-1α, MIP-1β, MCP-1, MCP-2, MCP-3 and I-309. The gene for human CCL17 has been mapped to chromosome 16q13 rather than chromosome 17 where the genes for many human CC chemokines are clustered. CCL17 is constitutively expressed in thymus, and at a lower level in lung, colon, and small intestine. CCL17 is also transiently expressed in stimulated peripheral blood mononuclear cells.
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CCL18, is a novel CC chemokine that is highly homologous to MIP-1α (61% amino acid sequence identity). CCL18 cDNA encodes an 89 aa residue precursor protein with a 20 aa putative signal peptide that is cleaved to generate a 69 aa residue mature protein which lacks potential glycosylation sites. In vitro, CCL18 mRNA expression is induced in alternatively activated macrophages by Th2 cytokines such as IL-4, IL-10 and IL-13, and inhibited by IFN-γ. CCL18 mRNA is also expressed by GM-CSF/IL-4-induced monocyte-derived dendritic cells. In vivo, CCL18 is highly expressed in lung and placenta but is not expressed in epidermal Langerhans cells. Recombinant CCL18 has been shown to chemoattract naive T cells, but not monocytes or neutrophils.