812 Results for: "MMP-9"

Supplier: Bioss

Matrix metalloproteinase 26 preprotein; gelatinase A; 70kD type IV collagenase; gelatinase neutrophil. Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes as well as in disease processes. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. MMP26 degrades type IV collagen, the major structural component of basement membranes. The enzyme plays a role in endometrial menstrual breakdown, regulation of vascularization and the inflammatory response.Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodelling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. MMP26, also known as Matrilysin 2, was first cloned from human fetal cells, and identified as an MMP most closely related to MMP7 (Matrilysin 1). The homology between MMP7 and MMP26 is low (only 38% identical), thus the functions are unlikely to be similar. Homology is much higher (48% identical) for the comparable region of MMP12, but MMP26 appears to have broader substrate specificity than does MMP12. MMP26, like MMP7, lacks the hemopexin domain common to the other MMPs, but contains a Propeptide domain, cysteine switch activation site, followed by a catalytic domain, and a short vestige of the hinge region. MMP26 is apparently not glycosylated, and is a secreted MMP. Tissue analysis shows MMP26 most strongly in placenta and uterus, but also in kidney cells, lung cells, lymphocytes and lung or endometrial carcinoma cells. MMP26 is proteolytically active, cleaving casein in zymograms, and gelatin, a1PI, fibrinogen, fibronectin, vitronectin, type IV collagen, and apparently activating MMP9.

Supplier: Bioss

Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. May form part of a tissue-specific acute response to remodeling stimuli. Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-9, MMP-13, MMP-14 and MMP-15.

Supplier: Bioss

Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. May form part of a tissue-specific acute response to remodeling stimuli. Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-9, MMP-13, MMP-14 and MMP-15.

Supplier: Bioworld Technology

Synthetic peptide, corresponding to amino acids 51-100 of Human MMP-23.

Supplier: ENZO LIFE SCIENCES

The matrix metalloproteinase (MMP) RED and GREEN Drug Discovery Kits are complete assay systems designed to screen MMP inhibitors, using long-wavelength quenched fluorogenic substrates OmniMMP™ RED or Fluorogenic Substrate (GREEN). The assays are performed in a convenient 96-well microplate format, with the compound NNGH also included as a prototypic control inhibitor.

Supplier: ENZO LIFE SCIENCES

Produced in E. coli. Mature human MMP-14 (aa 89-265).

Supplier: ENZO LIFE SCIENCES

A QuantiZyme™ Assay System. The MMP-8 Fluorometric (also known as fluorimetric) Drug Discovery Kit is a complete assay system designed to screen inhibitors of matrix metalloproteinase-8 (MMP-8, neutrophil collagenase, collagenase-2) using a quenched fluorogenic peptide: OmniMMP™ fluorogenic substrate Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2. Mca fluorescence is quenched by the Dpa group until cleavage by MMPs at the Gly-Leu bond separates the two moieties

Supplier: ENZO LIFE SCIENCES

A QuantiZyme™ Assay System. The MMP-12 Colorimetric Drug Discovery Kit is a complete assay system designed to screen inhibitors of matrix metalloproteinase-12 (MMP-12, macrophage elastase, metalloelastase) using a thiopeptide as a chromogenic substrate. The assays are performed in a convenient 96-well plate format. Included are active enzyme, assay buffer, a prototypic control inhibitor (NNGH), and a detailed instruction booklet.

Supplier: Bioss

Matrix metalloproteinase 26 preprotein; gelatinase A; 70kD type IV collagenase; gelatinase neutrophil. Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes as well as in disease processes. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. MMP26 degrades type IV collagen, the major structural component of basement membranes. The enzyme plays a role in endometrial menstrual breakdown, regulation of vascularization and the inflammatory response.Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodelling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. MMP26, also known as Matrilysin 2, was first cloned from human fetal cells, and identified as an MMP most closely related to MMP7 (Matrilysin 1). The homology between MMP7 and MMP26 is low (only 38% identical), thus the functions are unlikely to be similar. Homology is much higher (48% identical) for the comparable region of MMP12, but MMP26 appears to have broader substrate specificity than does MMP12. MMP26, like MMP7, lacks the hemopexin domain common to the other MMPs, but contains a Propeptide domain, cysteine switch activation site, followed by a catalytic domain, and a short vestige of the hinge region. MMP26 is apparently not glycosylated, and is a secreted MMP. Tissue analysis shows MMP26 most strongly in placenta and uterus, but also in kidney cells, lung cells, lymphocytes and lung or endometrial carcinoma cells. MMP26 is proteolytically active, cleaving casein in zymograms, and gelatin, a1PI, fibrinogen, fibronectin, vitronectin, type IV collagen, and apparently activating MMP9.

Supplier: Bioss

Matrix metalloproteinase 26 preprotein; gelatinase A; 70kD type IV collagenase; gelatinase neutrophil. Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes as well as in disease processes. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. MMP26 degrades type IV collagen, the major structural component of basement membranes. The enzyme plays a role in endometrial menstrual breakdown, regulation of vascularization and the inflammatory response.Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodelling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. MMP26, also known as Matrilysin 2, was first cloned from human fetal cells, and identified as an MMP most closely related to MMP7 (Matrilysin 1). The homology between MMP7 and MMP26 is low (only 38% identical), thus the functions are unlikely to be similar. Homology is much higher (48% identical) for the comparable region of MMP12, but MMP26 appears to have broader substrate specificity than does MMP12. MMP26, like MMP7, lacks the hemopexin domain common to the other MMPs, but contains a Propeptide domain, cysteine switch activation site, followed by a catalytic domain, and a short vestige of the hinge region. MMP26 is apparently not glycosylated, and is a secreted MMP. Tissue analysis shows MMP26 most strongly in placenta and uterus, but also in kidney cells, lung cells, lymphocytes and lung or endometrial carcinoma cells. MMP26 is proteolytically active, cleaving casein in zymograms, and gelatin, a1PI, fibrinogen, fibronectin, vitronectin, type IV collagen, and apparently activating MMP9.

Supplier: ENZO LIFE SCIENCES

A QuantiZyme™ Assay SystemThe MMP-9 Fluorometric (also known as fluorimetric) Drug Discovery Kit is a complete assay system designed to screen inhibitors of matrix metalloproteinase-9 (MMP-9, gelatinase B) using a quenched fluorogenic peptide: OmniMMP™ fluorogenic substrate Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH. Mca fluorescence is quenched by the Dpa group until cleavage by MMPs at the Gly-Leu bond separates the two moieties.

Supplier: ENZO LIFE SCIENCES

A QuantiZyme™ Assay System. The MMP-3 Fluorometric (also known as fluorimetric) Drug Discovery Kit is a complete assay system designed to screen inhibitors of matrix metalloproteinase-3 (MMP-3, stromelysin-1) using a quenched fluorogenic peptide: OmniMMP™ fluorogenic substrate Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH. Mca fluorescence is quenched by the Dpa group until cleavage by MMPs at the Gly-Leu bond separates the two moieties.

Supplier: Bioss

Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. Known to act on MMP-1, MMP-2, MMP-3, MMP-7 and MMP-9.

Supplier: Bioss

Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. Known to act on MMP-1, MMP-2, MMP-3, MMP-7 and MMP-9.

Supplier: US Biological

Anti-MMP-2, hinge region Rabbit Polyclonal Antibody

Supplier: Bioworld Technology

Recombinant full length Human MMP-13.

Supplier: Bioworld Technology

Recombinant full length Human MMP-11.

Supplier: Bioss

Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. Known to act on MMP-1, MMP-2, MMP-3, MMP-7 and MMP-9.

Supplier: Bioss

Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. Known to act on MMP-1, MMP-2, MMP-3, MMP-7 and MMP-9.

Supplier: Bioss

Matrix metalloproteinase 26 preprotein; gelatinase A; 70kD type IV collagenase; gelatinase neutrophil. Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes as well as in disease processes. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. MMP26 degrades type IV collagen, the major structural component of basement membranes. The enzyme plays a role in endometrial menstrual breakdown, regulation of vascularization and the inflammatory response.Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. MMP26, also known as Matrilysin 2, was first cloned from human fetal cells, and identified as an MMP most closely related to MMP7 (Matrilysin 1). The homology between MMP7 and MMP26 is low (only 38% identical), thus the functions are unlikely to be similar. Homology is much higher (48% identical) for the comparable region of MMP12, but MMP26 appears to have broader substrate specificity than does MMP12. MMP26, like MMP7, lacks the hemopexin domain common to the other MMPs, but contains a Propeptide domain, cysteine switch activation site, followed by a catalytic domain, and a short vestige of the hinge region. MMP26 is apparently not glycosylated, and is a secreted MMP. Tissue analysis shows MMP26 most strongly in placenta and uterus, but also in kidney cells, lung cells, lymphocytes and lung or endometrial carcinoma cells. MMP26 is proteolytically active, cleaving casein in zymograms, and gelatin, a1PI, fibrinogen, fibronectin, vitronectin, type IV collagen, and apparently activating MMP9.

Supplier: Bioss

Matrix metalloproteinase-7 (MMP-7) also known as matrilysin and PUMP (EC 3.4.24.23) cleaves a number of substrates including collagen types IV and X, elastin, fibronectin, gelatin, laminin and proteoglycans. MMP-7 is closely related to the stromelysin family members but is encoded by a different gene. MMP-7 is the smallest of all the MMPs consisting of a pro-peptide domain and a catalytic domain. It lacks the hemopexin-like domain common to other members of the MMPs. MMP-7 is secreted as a 28kD proenzyme and can be activated in vitro by organomercurials and trypsin and in vivo by MMP-3 to a 18kD active MMP-7 enzyme. Once activated, MMP-7 can activate pro-MMP-1 and pro-MMP-9 but not pro-MMP-2. MMP-7 is widely expressed having been reported in elevated levels in cycling endometrium as well as in colorectal cancers and adenomas, hepatocellular carcinomas, rectal carcinomas, and approximately 50% of gliomas.

Supplier: Bioworld Technology

Synthetic peptide, corresponding to amino acids 550-600 of Human MMP-16.

Supplier: ENZO LIFE SCIENCES

Specific non-chelating small-molecule inhibitor of MMP-12 (IC50 = 14 nM). At higher concentrations it inhibits other MMPs, but spares MMP-1, making it a valuable tool for investigation of MMP activity and function.

Supplier: ENZO LIFE SCIENCES

A QUANTIZYME® Assay System Complete assay system designed to examine the specificity of inhibitors against a panel of ten matrix metalloproteinase enzymes. The assays are performed in a convenient 96-well microplate format using a chromogenic substrate1,2 detected at 412 nm. Included are active MMP enzymes, assay buffer, a prototypic control inhibitor (NNGH3), and a detailed instruction booklet.

Supplier: Bioss

Negatively regulates matrix metalloproteinase-9 (MMP-9) by suppressing MMP-9 secretion and by direct inhibition of its enzymatic activity. RECK down-regulation by oncogenic signals may facilitate tumor invasion and metastasis. Appears to also regulate MMP-2 and MT1-MMP, which are involved in cancer progression.

Supplier: Bioss

Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. May form part of a tissue-specific acute response to remodeling stimuli. Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-9, MMP-13, MMP-14 and MMP-15.

Supplier: ENZO LIFE SCIENCES

A QUANTIZYME® Assay System Complete assay system designed to examine the specificity of inhibitors against a panel of ten matrix metalloproteinase enzymes. The assays are performed in a convenient 96-well microplate format using a sensitive fluorogenic substrate . Included are active MMP enzymes, assay buffer, a prototypic control inhibitor (NNGH3), and a detailed instruction booklet.

Supplier: Bioss

Negatively regulates matrix metalloproteinase-9 (MMP-9) by suppressing MMP-9 secretion and by direct inhibition of its enzymatic activity. RECK down-regulation by oncogenic signals may facilitate tumor invasion and metastasis. Appears to also regulate MMP-2 and MT1-MMP, which are involved in cancer progression.

Supplier: Bioworld Technology

Synthetic peptide, corresponding to amino acids 12-60 of Human MMP-19.

Supplier: Bioworld Technology

Synthetic peptide, corresponding to amino acids 351-400 of Human MMP-10.