ELISA

Chemokine(C-C motif) ligand 7(CCL7) is a small cytokine known as a chemokine that was previously called monocyte-specific chemokine 3(MCP3). It belongs to the C-C chemokine family. By fluorescence in situ hybridization, mapped the MCP3 gene to chromosome 17q11.2-q12. MCP3 was identified as a physiologic substrate of gelatinase A. Cleaved MCP3 binds to CC-chemokine receptors-1, -2, and -3, but no longer induces calcium fluxes or promotes chemotaxis, and instead acts as a general chemokine antagonist that dampens inflammation, suggested that matrix metalloproteinases are both effectors and regulators of the inflammatory response.

M-CSF, also called CSF1, has a role in development of the placenta. Uterine CSF1 concentration is regulated by a synergistic action of estradiol and progesterone. CSF1 is produced by uterine glandular epithelial cells. It had been found that FMS, the CSF1 receptor, is expressed in placenta and choriocarcinoma cell lines1. The CSF1 gene is mapped to 1p21-p13 and contains 10 exons and 9 introns spanning 20 kb2. And there are 2 forms of CSF1, with 224 and 522 amino acids, resulting from alternative splicing3.

M-CSF, also called CSF1, consists of a 14-amino acid peptide, longer than the usual 8-to-11 mer recognized by most CTLs. The M-CSF gene is mapped to 1p21-p13 and contains 10 exons and 9 introns spanning 20 kb1. Although it is a single-copy gene, its expression results in the synthesis of several mRNAs, ranging in size from about 1.5 to 4.5 kb2. There are 2 forms of M-CSF, with 224 and 522 amino acids, resulting from alternative splicing3. Furthermore, M-CSF has a role in development of the placenta. Uterine M-CSF concentration is regulated by a synergistic action of estradiol and progesterone. M-CSF is produced by uterine glandular epithelial cells. It had been found that FMS, the M-CSF receptor, is expressed in placenta and choriocarcinoma cell lines4.

Macrophage-derived chemokine(MDC), also called Chemokine, cc motif, ligand 22(CCL22) or Small inducible cytokine subfamily A, member 22(SCY22). MDC is a recently identified member of the CC chemokine family. It is not closely related to other chemokines, sharing most similarity with thymus- and activation-regulated chemokine(TARC), which contains 37% identical amino acids. In addition, MDC gene is mapped to chromosome 16q13, the same position reported for the TARC gene. MDC has the four-cysteine motif and other highly conserved residues characteristic of CC chemokines, but it shares<35% identity with any of the known chemokines. Recombinant MDC was expressed in Chinese hamster ovary cells and purified by heparin-Sepharose chromatography. MDC is highly expressed in macrophages and in monocyte-derived dendritic cells, but not in monocytes, natural killer cells, or several cell lines of epithelial, endothelial, or fibroblast origin. High expression was also detected in normal thymus and l

Macrophage-derived chemokine(MDC), also called Chemokine, cc motif, ligand 22(CCL22) or Small inducible cytokine subfamily A, member 22(SCY22). MDC is a recently identified member of the CC chemokine family. It is not closely related to other chemokines, sharing most similarity with thymus- and activation-regulated chemokine(TARC), which contains 37% identical amino acids. In addition, MDC gene is mapped to chromosome 16q13, the same position reported for the TARC gene. MDC has the four-cysteine motif and other highly conserved residues characteristic of CC chemokines, but it shares<35% identity with any of the known chemokines. Recombinant MDC was expressed in Chinese hamster ovary cells and purified by heparin-Sepharose chromatography. MDC is highly expressed in macrophages and in monocyte-derived dendritic cells, but not in monocytes, natural killer cells, or several cell lines of epithelial, endothelial, or fibroblast origin. High expression was also detected in normal thymus and l

Macrophage inflammatory protein-1 alpha(MIP-1 alpha), also called CCL3, LD78. The cDNA for MIP-1 alpha predicts a mature peptide of 69 amino acids with a molecular mass of 7,889 daltons. LD78 is a member of a newly identified superfamily of small inducible proteins involved in inflammatory responses, wound healing and tumorigenesis. MIP-1 alpha is a chemokine that has pro-inflammatory and stem cell inhibitory activities in vitro. It constitutes an important second signal for mast cell degranulation in the conjunctiva in vivo and consequently for acute-phase disease. The standard product used in this kit is recombinant human MIP-1alpha, consisting of 66 amino acids with the molecular mass of 7.5kDa.

Chemokine(C-C motif) ligand 3(CCL3), so known as Macrophage inflammatory protein-1alpha(MIP-1 alpha), is a protein that in humans is encoded by the CCL3 gene. It is a cytokine which belongs to the CC chemokine family that is involved in the acute inflammatory state in the recruitment and activation of polymorphonuclear leukocytes. This gene is mapped to 17q12. CCL3 plays a role in inflammatory responses through binding to the receptors CCR1, CCR4 and CCR5. It has been found that the activation of CCR5 by CCL3 directly and independently activates a G-protein signaling pathway through GNAI2 and a tyrosine phosphorylation signaling pathway through JAK2.

Chemokine(C-C motif) ligand 4, also known as CCL4, is a protein which in humans is encoded by the CCL4 gene. It is a CC chemokine with specificity for CCR5 receptors. It is a chemoattractant for natural killer cells, monocytes and a variety of other immune cells. CCL4 is a major HIV-suppressive factor produced by CD8+ T cells. Performing-low memory CD8+ T cells that normally synthesize MIP-1-beta. the CCL4 gene was assigned to a slightly more distal location: 17q21-q23 rather than 17q11-q21.

MIP is a member of the aquaporin family of membrane-bound water channels. MIP family proteins are thought to contain 6 TM domains. Sequence analysis suggests that the proteins may have arisen through tandem, intragenic duplication from an ancestral protein that contained 3 TM domains. Major intrinsic protein(MIP, also called MP26) is the predominant fiber cell membrane protein of the ocular lens. The major intrinsic protein(MIP) of the vertebrate eye lens is the first identified member of a sequence-related family of cell-membrane proteins that appears to have evolved by gene duplication. Several members of the MIP family transport water(aquaporins), glycerol and other small molecules in microbial, plant and animal cells. The standard used in this kit is recombinant mouse MIP-2(A28-N100), consisting of 73 amino acids with the molecular mass of 8KDa.