814 Results for: "MMP-9"

Supplier: ENZO LIFE SCIENCES

Cell-permeable, potent, selective, and reversible MMP-9 inhibitor.

Supplier: ENZO LIFE SCIENCES

Inhibitor of matrix metalloproteinase 3 (MMP-3) (IC50=5µM).

Supplier: Merck Millipore (Calbiochem‎)

A piperazine-based, cell-permeable, and highly potent inhibitor of MMP-9 (IC₅₀=900 pM) and MMP-13 (IC₅₀=900 pM).

Supplier: ENZO LIFE SCIENCES

Potent MMP-13 inhibitor.

Supplier: ENZO LIFE SCIENCES

A novel and selective inhibitor of MMP-13 (89% at 33 µM). Acts via binding to the S1' pocket of MMP-13 without metal chelation.

Supplier: ENZO LIFE SCIENCES

Sensitive chromogenic MMP substrate

Supplier: ENZO LIFE SCIENCES

MMP-1 assay buffer

Supplier: ENZO LIFE SCIENCES

Fluorogenic substrate for several matrix metalloproteinases (MMPs).

Supplier: ENZO LIFE SCIENCES

MMP-3 Fluorescent assay buffer

Supplier: ENZO LIFE SCIENCES

MMP-1 colorimetric assay buffer

Supplier: ENZO LIFE SCIENCES

Fluorogenic substrate for several matrix metalloproteinases (MMPs).

Supplier: ENZO LIFE SCIENCES

Produced in insect cells. Primarily full length latent MMP-13, with some active forms present.

Supplier: Bioworld Technology

Recombinant full length Human MMP-8.

Supplier: Bioworld Technology

Recombinant full length Human MMP-7.

Supplier: Bioworld Technology

Recombinant full length Human MMP-1.

Supplier: Bioworld Technology

Recombinant full length Human MMP-10.

Supplier: Novus Biologicals

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.

Supplier: Bioworld Technology

Recombinant full length Human MMP-13.

Supplier: Bioworld Technology

Recombinant full length Human MMP-11.

Supplier: AAT BIOQUEST

The matrix metalloproteinases (MMPs) constitute a family of zinc-dependent endopeptidases that function within the extracellular matrix.

Supplier: ENZO LIFE SCIENCES

The MMP inhibitor profiling kit, fluorometric RED is a complete assay system designed to examine the specificity of inhibitors against a panel of ten matrix metalloproteinase enzymes, using a quenched fluorogenic substrate OMNIMMP® RED.

Supplier: AAT BIOQUEST

The matrix metalloproteinases (MMPs) constitute a family of zinc-dependent endopeptidases that function within the extracellular matrix.

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: AAT BIOQUEST

The matrix metalloproteinases (MMPs) constitute a family of zinc-dependent endopeptidases that function within the extracellular matrix.

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: 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

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 415-460 of Human MMP-8.

Supplier: US Biological

Anti-MMP-2, hinge region Rabbit Polyclonal Antibody

Supplier: Bioworld Technology

Synthetic peptide, corresponding to amino acids 601-650 of Human MMP-2.