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: 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

MMP-1 assay buffer

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: 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, MMP-8, MMP-9, MMP-1, MMP-13, MMP-14, MMP-15, MMP-16 and MMP-19.

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, MMP-8, MMP-9, MMP-1, MMP-13, MMP-14, MMP-15, MMP-16 and MMP-19.

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, MMP-8, MMP-9, MMP-1, MMP-13, MMP-14, MMP-15, MMP-16 and MMP-19.

Supplier: ENZO LIFE SCIENCES

MMP-3 Fluorescent assay buffer

Supplier: ENZO LIFE SCIENCES

A QuantiZyme™ Assay System. The MMP-2 Colorimetric Drug Discovery Kit is a complete assay system designed to screen inhibitors of matrix metalloproteinase-2 (MMP-2, gelatinase A) using a thiopeptide as a chromogenic substrate. The assays are performed in a convenient 96-well microplate format. The kit is useful to screen inhibitors of MMP-2, a potential therapeutic target.

Supplier: ENZO LIFE SCIENCES

Sensitive chromogenic MMP substrate

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 601-650 of Human MMP-2.

Supplier: ENZO LIFE SCIENCES

MMP-1 colorimetric assay buffer

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-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: 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, MMP-8, MMP-9, MMP-1, MMP-13, MMP-14, MMP-15, MMP-16 and MMP-19.

Supplier: ENZO LIFE SCIENCES

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

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, MMP-8, MMP-9, MMP-1, MMP-13, MMP-14, MMP-15, MMP-16 and MMP-19.

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, MMP-8, MMP-9, MMP-1, MMP-13, MMP-14, MMP-15, MMP-16 and MMP-19.

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, MMP-8, MMP-9, MMP-1, MMP-13, MMP-14, MMP-15, MMP-16 and MMP-19.

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, MMP-8, MMP-9, MMP-1, MMP-13, MMP-14, MMP-15, MMP-16 and MMP-19.

Supplier: ENZO LIFE SCIENCES

A QuantiZyme™ Assay System. The MMP-10 Fluorometric (also known as fluorimetric) Drug Discovery Kit is a complete assay sytem designed to screen for inhibitors of matrix metalloproteinase-10 (MMP-10, stromelysin-2) 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: Bioworld Technology

Recombinant full length Human MMP-8.

Supplier: ENZO LIFE SCIENCES

Fluorogenic substrate for several matrix metalloproteinases (MMPs).

Supplier: ENZO LIFE SCIENCES

Fluorogenic substrate for several matrix metalloproteinases (MMPs).

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: ENZO LIFE SCIENCES

A QuantiZyme™ Assay System. The MMP-1 Colorimetric Drug Discovery Kit is a complete assay system designed to screen inhibitors of matrix metalloproteinase-1 (MMP-1, interstitial collagenase, fibroblast collagenase) using a thiopeptide as a chromogenic substrate.