Anti-Human CCL-7 Antibody
755.99 €
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Catalog number: 209 - 101-M275
Product Category: Business & Industrial > Science & Laboratory
Gentaur
Size: 100 µg
101-M275
Anti-Human CCL-7 Antibody
MCP2 and CCL7 are two monocyte chemotactic proteins produced by human MG63 osteosarcoma cells. Both MCP2 and CCL7 are members of the CC family of chemokines and share 62% and 71% amino acid sequence identity, respectively, with MCP1. CCL7 also shares 58% amino acid identity with MCP2. CCL7 cDNA encodes a 99 amino acid residue precursor protein from which the N-terminal 23 amino acid residues are cleaved to generate the 76 amino acid residue mature CCL7. Mature CCL7 contains a potential N-linked and several possible O-linked glycosylation sites. Similarly to other CC chemokines, all three MCP proteins are monocyte chemoattractants. In addition, the three MCPs can chemoattract activated NK cells as well as CD4+ and CD8+ T lymphocytes. All three cytokines have also been shown to attract eosinophils and induce histamine secretion from basophils.
755.99 €
103-M331
Anti-Mouse CCL-27 Antibody
CCL27, also known as CTACK (cutaneous T cel-lattracting chemokine), ALP, ILC, and ESkine, is a member of the CC family of chemokines. Mature mouse CCL27 is a 95 amino acid (aa) protein that shares 57% aa and 87% aa sequence identity with human and rat CCL27, respectively. It shares 18-31% aa sequence identity with other mouse CC chemokines. An alternately spliced form of mouse CCL27, known as PESKY, is localized to the nucleus and promotes cellular migration. CCL27 is constitutively expressed by keratinocytes and is upregulated by inflammatory stimuli and in wounded skin. CCL27 binds the chemokine receptor CCR10, glycosaminoglycans in the extracellular matrix, sulfated tyrosine residues on PSGL1, and determinants on the surface of fibroblasts and endothelial cells. CCL27 cooperates with CCL17/TARC in inducing the migration of cutaneous lymphocyte antigen (CLA) positive memory T cells to the skin during inflammation. Endothelial cellbound CCL27 can mediate the adhesion of those cells to CLA+ T cells. CCL27 also induces the migration of keratinocyte precursors from bone marrow to the skin, thereby promoting wound healing. In humans, serum CCL27 levels are elevated and correlate with disease severity in atopic dermatitis, psoriasis vulgaris, and mycosis fungoides.
755.99 €
103-M332
Anti-Mouse CCL-28 Antibody
Mouse CCL28 (CC chemokine ligand 28) is a novel CC chemokine cloned from a Rag1 mouse kidney cDNA library. Mouse CCL28 cDNA encodes a 130 amino acid (aa) precursor protein with a 22 aa signal peptide and a 108 aa mature protein. Mature human and mouse CCL28 share 83% aa identity. Among CC chemokines, CCL28 shares the most homology with CCL27/CTACK. Mouse CCL28 is produced by epithelial cells. Based on Northern blot analysis, it is mainly expressed in testes, kidney and brain. The receptor for CCL28 has been identified as the CCR10, which is also the receptor for CCL27/CTACK.
755.99 €
103-M333
Anti-Mouse CCL-3 Antibody
The macrophage inflammatory proteins 1α (or CCL3) and 1β, two closely related but distinct proteins, were originally co purified from medium conditioned by a LPS-stimulated murine macrophage cell line. Mature mouse MIP1α shares approximately 77% and 70% amino acid identity with human MIP1α and mouse MIP1β, respectively. MIP1 proteins are expressed primarily in T cells, B cells, and monocytes after antigen or mitogen stimulation. The MIP1 proteins are members of the β (CC) subfamily of chemokines. Both MIP1α and MIP1β are monocyte chemoattractants in vitro. Additionally, the MIP1 proteins have been reported to have chemoattractant and adhesive effects on lymphocytes, with MIP1α and MIP1β preferentially attracting CD8+ and CD4+ T cells, respectively. MIP1α has also been shown to attract B cells as well as eosinophils. MIP1 proteins have been reported to have multiple effects on hematopoietic precursor cells and MIP1α has been identified as a stem cell inhibitory factor that can inhibit the proliferation of hematopoietic stem cells in vitro as well as in vivo. In the same assays, MIP1β was reported to be much less active. The functional receptor for MIP1α has been identified as CCR1 and CCR5.