You Searched For: CL-82198+(MMP-13+inhibitor)


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Catalog Number: (89151-270)
Supplier: Enzo Life Sciences
Description: Selective and cell permeable inhibitor of the interaction between the human eukaryotic translation initiation factors 4E (eIF4E) and 4G (eIF4G).


Supplier: Bachem Americas
Description: Sequence: 4-Abz-Gly-Pro-D-Leu-D-Ala-NHOH
Synonym(s): MMP Inhibitor 1

Catalog Number: (75791-486)
Supplier: Prosci
Description: Metalloproteinase inhibitor 4 is an enzyme that in humans is encoded by the TIMP4 gene, belongs to the protease inhibitor I35 (TIMP) family. The protein 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: Enzo Life Sciences
Description: MMP inhibitor

Supplier: Enzo Life Sciences
Description: Competitive, mechanism-based inhibitor of matrix metalloproteinases 2 and 9 (MMP-2 and MMP-9). It possesses Ki values in the nanomolar range against the gelatinases (14nM for MMP-2; 600nM for MMP-9), but in the micromolar range against other metalloproteinases (206µM for MMP-1, 15µM for MMP-3, 96µM for MMP-7, and 4µM for ADAM17/TACE). This inhibitor has also been used in vitro, in vivo, and in tissue culture. In vivo, it is metabolized to an even more potent gelatinase inhibitor.

Catalog Number: (103010-412)
Supplier: Anaspec Inc
Description: Matrix metalloproteinases (MMPs) belong to a family of secreted or membrane-associated proteins capable of digesting extracellular matrix components


Supplier: Anaspec Inc
Description: Matrix metalloproteinases (MMPs) belong to a family of secreted or membrane-associated zinc endopeptidases capable of digesting extracellular matrix components. MMP-12 (macrophage elastase) is involved in smoke-induced emphysema, tumor and other diseases. MMP-12 is secreted as a 54-kDa zymogen and becomes the mature 45-kDa active form after proteolytic cleavage. MMP-12 has a broad range of substrates, including α-1 proteinase inhibitor, α-2 antiplasmin, plasminogen activator inhibitor-2, collagen IV, laminin, fibronectin, elastin, but not interstitial collagens.

The sequence (Accession # NP_002417) corresponding to the catalytic domain (aa 106-267) of Human MMP-12 was expressed in E. coli. The recombinant human MMP-12 was purified from bacterial lysate and refolded using proprietary technique. The molecular weight of the recombinant Human MMP-12 Catalytic Domain is 18 kDa.

Catalog Number: (89156-416)
Supplier: Enzo Life Sciences
Description: 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 412nm. Included are active MMP enzymes, assay buffer, a prototypic control inhibitor (NNGH3), and a detailed instruction booklet.


Supplier: Enzo Life Sciences
Description: MMP inhibitor

Catalog Number: (89156-418)
Supplier: Enzo Life Sciences
Description: 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.


Catalog Number: (89161-656)
Supplier: Enzo Life Sciences
Description: MMP inhibitor


Catalog Number: (89156-462)
Supplier: Enzo Life Sciences
Description: A QuantiZymeTM Assay SystemThe MMP-7 Colorimetric Drug Discovery Kit is a complete assay system designed to screen inhibitors of matrix metalloproteinase-7 (MMP-7, matrilysin) using a thiopeptide as a chromogenic substrate.


Catalog Number: (CA80001-978)
Supplier: MilliporeSigma
Description: Full-length, recombinant, human pro-MMP-2 expressed in mouse cells that is subsequently activated by APMA. APMA is removed through a desalting column. The substrate specificity for MMP-2 includes collagen (types IV, V, VII, and X), elastin, and gelatin (type I). The presence of TIMP-2 inhibitor prevents degradation of the MMP-2 C-terminal regulatory domain. TIMP-2 is also an inhibitor of proteolysis and will inhibit the activity of the enzyme. Useful for immunoblotting, substrate cleavage assay and zymography. Matrix metalloproteinases are members of a unique family of proteolytic enzymes that have a zinc ion at their active sites and can degrade collagens, elastin and other components of the extracellular matrix (ECM). These enzymes are present in normal healthy individuals and have been shown to have an important role in processes such as wound healing, pregnancy, and bone resorption. However, overexpression and activation of MMPs have been linked with a range of pathological processes and disease states involved in the breakdown and remodeling of the ECM. Such diseases include tumor invasion and metastasis, rheumatoid arthritis, periodontal disease, and vascular processes such as angiogenesis, intimal hyperplasia, atherosclerosis, and aneurysms. Recently, MMPs have been linked to neurodegenerative diseases such as Alzheimer′s, and amyotrophic lateral sclerosis (ALS). Natural inhibitors of MMPs, tissue inhibitor of matrix metalloproteinases (TIMPs) exist and synthetic inhibitors have been developed which offer hope of new treatment options for these diseases. Regulation of MMP activity can occur at the level of gene expression, including transcription and translation, level of activation, or at the level of inhibition by TIMPs. Thus, perturbations at any of these points can theoretically lead to alterations in ECM turnover. Expression is under tight control by pro- and anti-inflammatory cytokines and/or growth factors and, once produced the enzymes are usually secreted as inactive zymograms. Upon activation (removal of the inhibitory propeptide region of the molecules) MMPs are subject to control by locally produced TIMPs. All MMPs can be activated in vitro with organomercurial compounds (e.g., 4-aminophenylmercuric acetate), but the agents responsible for the physiological activation of all MMPs have not been clearly defined. Numerous studies indicate that members of the MMP family have the ability to activate one another. The activation of the MMPs in vivo is likely to be a critical step in terms of their biological behavior, because it is this activation that will tip the balance in favor of ECM degradation. The hallmark of diseases involving MMPs appear to be stoichiometric imbalance between active MMPs and TIMPs, leading to excessive tissue disruption and often degradation. Determination of the mechanisms that control this imbalance may open up some important therapeutic options of specific enzyme inhibitors.

Catalog Number: (89161-702)
Supplier: Enzo Life Sciences
Description: 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.


Catalog Number: (89161-662)
Supplier: Enzo Life Sciences
Description: MMP inhibitor


Catalog Number: (89358-832)
Supplier: Genetex
Description: Matrix metalloproteinases (MMPs) are a family of enzymes that are responsible for the degradation of extracellular matrix components such as collagen, laminin and proteoglycans. These enzymes are involved in normal physiological processes such as embryogenesis and tissue remodeling and may play an important role in arthritis, periodontitis, and metastasis.The activation and activity of MMPs are regulated by a family of endogenous inhibitors, tissue inhibitors of metalloproteinase (TIMP). TIMP2 (also called CSC-21K) is a 21 kDa glycoprotein that is expressed by a variety of cell types. It forms a non-covalent, stoichiometric complex with both latent and active MMPs. TIMP2 shows a preference for MMP-2. TIMPs are capable of altering the metastatic potential of cancer cells and have been shown to inhibit invasion and metastasis in animal models.


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