ELISA

Macrophage Inflammatory Protein 3alpha(MIP3alpha), also called Chemokine, cc motif, ligand 20(CCL20). The MIP-3alpha/CCL20 gene was cloned and sequenced, revealing a four exon, three intron structure, and was localized by FISH analysis to 2q35-q36. MIP3alpha is predominantly expressed in lymph nodes, appendix, PBL, fetal liver, fetal lung and several cell lines. MIP3alpha/CCL20 and its receptor CCR6 are markedly up-regulated in psoriasis, and they may play a role in the recruitment of T cells to lesional psoriatic skin. And Alanine MIP-3alpha and Serine MIP-3alpha, the two forms of MIP3alpha, that differ by one amino acid at the predicted signal peptide cleavage site. Both of them were chemically synthesized and tested for biological activity. And both flu antigen plus IL-2-activated CD4(+) and CD8(+) T lymphoblasts and cord blood-derived dendritic cells responded to Ser and Ala MIP-3alpha.

Macrophage Inflammatory Protein 3alpha(MIP3alpha), also called Chemokine, cc motif, ligand 20(CCL20). The MIP-3alpha/CCL20 gene was cloned and sequenced, revealing a four exon, three intron structure, and was localized by FISH analysis to 2q35-q36. MIP3alpha is predominantly expressed in lymph nodes, appendix, PBL, fetal liver, fetal lung and several cell lines. MIP3alpha/CCL20 and its receptor CCR6 are markedly up-regulated in psoriasis, and they may play a role in the recruitment of T cells to lesional psoriatic skin. And Alanine MIP-3alpha and Serine MIP-3alpha, the two forms of MIP3alpha, that differ by one amino acid at the predicted signal peptide cleavage site. Both of them were chemically synthesized and tested for biological activity. And both flu antigen plus IL-2-activated CD4(+) and CD8(+) T lymphoblasts and cord blood-derived dendritic cells responded to Ser and Ala MIP-3alpha.

Macrophage Inflammatory Protein 3alpha(MIP3alpha), also called Chemokine, cc motif, ligand 20(CCL20). The MIP-3alpha/CCL20 gene was cloned and sequenced, revealing a four exon, three intron structure, and was localized by FISH analysis to 2q35-q36. MIP3alpha is predominantly expressed in lymph nodes, appendix, PBL, fetal liver, fetal lung and several cell lines. MIP3alpha/CCL20 and its receptor CCR6 are markedly up-regulated in psoriasis, and they may play a role in the recruitment of T cells to lesional psoriatic skin. And Alanine MIP-3alpha and Serine MIP-3alpha, the two forms of MIP3alpha, that differ by one amino acid at the predicted signal peptide cleavage site. Both of them were chemically synthesized and tested for biological activity. And both flu antigen plus IL-2-activated CD4(+) and CD8(+) T lymphoblasts and cord blood-derived dendritic cells responded to Ser and Ala MIP-3alpha.

Chemokine(C-C motif) ligand 19(CCL19) is a small cytokine belonging to the CC chemokine family that is also known as EBI1 ligand chemokine(ELC) and macrophage inflammatory protein-3-beta (MIP-3-beta). Using PCR of human-rodent hybrids, the CCL19 gene was map to human chromosome 9p13, and the CCL19 gene is not part of the CC chemokine gene cluster on chromosome 17. The cytokine encoded by this gene may play a role in normal lymphocyte recirculation and homing. It also plays an important role in trafficking of T cells in thymus, and in T cell and B cell migration to secondary lymphoid organs.

Chemokine(C-C motif) ligand 19 (CCL19) is a small cytokine belonging to the CC chemokine family that is also known as EBI1 ligand chemokine (ELC) and macrophage inflammatory protein-3-beta (MIP-3-beta). Using PCR of human-rodent hybrids, the CCL19 gene was mapped to human chromosome 9p13, and the CCL19 gene is not part of the CC chemokine gene cluster on chromosome 17. The cytokine encoded by this gene may play a role in normal lymphocyte recirculation and homing. It also plays an important role in trafficking of T cells in thymus, and in T cell and B cell migration to secondary lymphoid organs.

Matrix metalloproteinase-1(MMP-1) is also known as collagenase. Matrix metalloproteinases(MMPs) are zinc-dependent proteases that degrade extrMMP-1llular matrix proteins. The MMPs comprise a family of at least 20 proteolytic enzymes that play an essential role in tissue remodeling. Matrix metalloproteinase-1(MMP-1) plays an important role in the degradation of collagen in inflammatory diseases. MMP1(interstitial collagenase), MMP9(gelatinase B) and MMP12(macrophage elastase) are thought to be important in the development of emphysema. Smoking-induced MMP-1 might be important in the skin-ageing effects of tobacco smoking. The standard product used in this kit is human MMP-1 with the molecular mass of 51-53KDa. The detected MMP-1 includes zymogen and active enzyme.

Type IV collagenase, 72-kD, is officially designated matrix metalloproteinase-2(MMP2). It is also known as gelatinase, 72-kD. MMP-2 plays an essential role in angiogenesis and arteriogenesis, two processes critical to restoration of tissue perfusion after ischemia. MMP-2 expression is increased in tissue ischemia, but the responsible mechanisms remain unknown. Matrix metalloproteinases(MMPs) catalyze extracellular matrix degradation. Control of their activity is a promising target for therapy of diseases characterized by abnormal connective tissue turnover. MMPs are expressed as latent proenzymes that are activated by proteolytic cleavage that triggers a conformational change in the propeptide(cysteine switch). The structure of proMMP-2 reveals how the propeptide shields the catalytic cleft and that the cysteine switch may operate through cleavage of loops essential for propeptide stability. The gene is localized to 16q21 using somatic cell hybrids and in situ hybridization. The standa

Type IV collagenase, 72-kD, is officially designated matrix metalloproteinase-2(MMP2). It is also known as gelatinase, 72-kD. MMP-2 plays an essential role in angiogenesis and arteriogenesis, two processes critical to restoration of tissue perfusion after ischemia. MMP-2 expression is increased in tissue ischemia, but the responsible mechanisms remain unknown. Matrix metalloproteinases(MMPs) catalyze extracellular matrix degradation. Control of their activity is a promising target for therapy of diseases characterized by abnormal connective tissue turnover. MMPs are expressed as latent proenzymes that are activated by proteolytic cleavage that triggers a conformational change in the propeptide(cysteine switch). The structure of proMMP-2 reveals how the propeptide shields the catalytic cleft and that the cysteine switch may operate through cleavage of loops essential for propeptide stability. The gene is localized to 16q21 using somatic cell hybrids and in situ hybridization. The standa

Matrix metalloproteinase-3(MMP-3) also called stromelysin or transin, is a proteoglycanase closely related to collagenase(MMP1) with a wide range of substrate specificities. The complete primary structure for human MMP-3, which has 477 residues including a 17-residue signal peptide. MMP-3 and collagenase are 54% identical in sequence, suggesting a common origin for the evolution of the two proteinases. MMP-3 and collagenase expression are coordinately modulated in synovial fibroblast cultures. MMP-3 is a secreted metalloprotease produced predominantly by connective tissue cells. Together with other metalloproteases, it can synergistically degrade the major components of the extracellular matrix. It is capable of degrading proteoglycan, fibronectin, laminin, and type IV collagen, but not interstitial type I collagen. MMP-3 genotype may be an important determinant of vascular remodeling and age-related arterial stiffening, with the heterozygote having the optimal balance between matrix a