ELISA Kits

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

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

Matrix metalloproteinase-7(MMP-7) previously called putative metalloproteinase I(PUMP1) or matrilysin. The PUMP1 gene has been identified through studies of collagenase-related connective-tissue-degrading metalloproteinases produced by human tumors. The PUMP I protein has 267 amino acids and is significantly shorter than stromelysin or collagenase(477 and 469 amino acids, respectively). Matrix metalloproteinases play a crucial role in tumor invasion and metastasis. Matrilysin, a member of the matrix metalloproteinase family, is structurally different from the other matrix metalloproteinases by virtue of the absence of a conserved COOH-terminal protein domain. In addition, matrilysin mRNA is regulated in a specific and distinct manner in normal and malignant tissues. Matrilysin has been shown to correlate with nodal or distant metastasis in colorectal carcinomas; however, its implication in early invasive colorectal carcinomas has not been determined.1 Matrilysin is also a mediator of p

Matrix metalloproteinase 8(MMP8) also called neutrophil collagenase. Neutrophil collagenase, a member of the family of matrix metalloproteinases, is distinct from the collagenase of skin fibroblasts and synovial cells in substrate specificity and immunologic cross reactivity. MMP8, an enzyme that degrades fibrillar collagens imparting strength to the fetal membranes, is expressed by leukocytes and chorionic cytotrophoblast cells. The human neutrophil collagenase(HNC) cDNA clone has been sequenced and shown to encode a 467-residue protein. Neutrophil collagenase has been found to possess 57% identity with the deduced protein sequence for fibroblast collagenase with 72% chemical similarity. Certain regions of the molecule, including the putative zinc-binding region, are highly conserved. When compared with the published sequence for fibroblast collagenase, neutrophil collagenase contains four additional sites for glycosylation. The standard product used in this kit is natural, isolating