ELISA

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

The 92-kD type IV collagenase is also known as 92-kD gelatinase, type V collagenase, gelatinase B, or matrix metalloproteinase-9(MMP9). The 72- and 92-kDa type IV collagenases are members of a group of secreted zinc metalloproteases. The matrix metalloproteinases(MMPs) are able to degrade the extracellular matrix and allow angiogenesis and tumor invasion. Gelatinase B, a matrix metalloproteinase that has proteolytic activity against connective tissue proteins, has been suggested to be important in the connective tissue remodeling processes associated with atherogenesis and plaque rupture. MMP-9 is predominantly expressed in neutrophils, macrophages, and mast cells, rather than in oncogene-positive neoplastic cells. The polymorphism of MMP-9 acts as a genetic factor for the development of smoking-induced pulmonary emphysema. The standard product used in this kit is recombinant human MMP-9 with the molecular mass of 95KDa. The detected MMP-9 includes zymogen and active enzyme.

The 92-kD type IV collagenase is also known as 92-kD gelatinase, type V collagenase, gelatinase B, or matrix metalloproteinase-9(MMP9). The 72- and 92-kDa type IV collagenases are members of a group of secreted zinc metalloproteases.1 The matrix metalloproteinases(MMPs) are able to degrade the extracellular matrix and allow angiogenesis and tumor invasion. Gelatinase B, a matrix metalloproteinase that has proteolytic activity against connective tissue proteins, has been suggested to be important in the connective tissue remodeling processes associated with atherogenesis and plaque rupture. MMP-9 is predominantly expressed in neutrophils, macrophages, and mast cells, rather than in oncogene-positive neoplastic cells. The polymorphism of MMP-9 acts as a genetic factor for the development of smoking-induced pulmonary emphysema.

Collagenase 3 is an enzyme that in humans is encoded by the MMP13 gene. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. The protein encoded by this gene cleaves type II collagen more efficiently than types I and III. The expression of MMP13 in osteoarthritic cartilage and its activity against type II collagen indicates that the enzyme plays a significant role in cartilage collagen degradation and must, therefore, form part of a complex target for proposed therapeutic interventions based on collagenase inhibition. It may be involved in articular cartilage turnover and cartilage pathophysiology associated with osteoarthritis. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3.

Nerve growth factor(NGF) is a polypeptide involved in the regulation of growth and differentiation of sympathetic and certain sensory neurons. NGF is thought to have a profound effect on the development and maintenance of sympathetic and embryonic sensory neurones. NGF activity isolated from the male mouse submaxillary gland(MSG) consists of three types of subunits, alpha, beta and gamma, which specifically interact to form a 7S, approximately 130,000-molecular weight(Mr) complex. The 7S complex contains two identical 118-amino acid beta-chains, which are solely responsible for the nerve growth-stimulating activity of NGF. NGF, which is expressed by inflammatory cells and effects changes that lead to increased neural responsiveness, could be a pivotal mediator in allergic rhinitis. The standard product used in this kit is human 2.5S NGF, which is a dimmer linking with two polypeptide chains of 120 amino acids.

Nerve growth factor(NGF) is a polypeptide involved in the regulation of growth and differentiation of sympathetic and certain sensory neurons. NGF is thought to have a profound effect on the development and maintenance of sympathetic and embryonic sensory neurones. NGF activity isolated from the male mouse submaxillary gland(MSG) consists of three types of subunits, alpha, beta and gamma, which specifically interact to form a 7S, approximately 130,000-molecular weight(Mr) complex. The 7S complex contains two identical 118-amino acid beta-chains, which are solely responsible for the nerve growth-stimulating activity of NGF. NGF, which is expressed by inflammatory cells and effects changes that lead to increased neural responsiveness, could be a pivotal mediator in allergic rhinitis.

Nerve growth factor(NGF) is a polypeptide involved in the regulation of growth and differentiation of sympathetic and certain sensory neurons. NGF is thought to have a profound effect on the development and maintenance of sympathetic and embryonic sensory neurones. NGF activity isolated from the male mouse submaxillary gland(MSG) consists of three types of subunits, alpha, beta and gamma, which specifically interact to form a 7S, approximately 130,000-molecular weight(Mr) complex. The 7S complex contains two identical 118-amino acid beta-chains, which are solely responsible for the nerve growth-stimulating activity of NGF. NGF, which is expressed by inflammatory cells and effects changes that lead to increased neural responsiveness, could be a pivotal mediator in allergic rhinitis.