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Catalog Number: (75791-768)

Supplier: Prosci

Description: Tissue Inhibitor of Metalloproteinases 1 (TIMP-1) complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. Also mediates erythropoiesis in vitro; but, unlike IL-3, it is species-specific, stimulating the growth and differentiation of only human and murine erythroid progenitors. Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-8, MMP-9, MMP-10, MMP-11, MMP-12, MMP-13, and MMP-16. TIMP-1 does not act on MMP-14.

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: (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.

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Catalog Number: (89161-662)

Supplier: Enzo Life Sciences

Description: MMP inhibitor

Supplier: Peprotech

Description: TIMP-1 is an extracellular inhibitor of MMPs, including MMP-1, -2, -3, -7, -8, -9, -10, -11, -12, -13, and -16. It belongs to the I35 (TIMP) family of irreversible protease inhibitors that function as key modulators of extracellular matrix degradation during tissue development and remodeling. TIMP-1 can also act through an MMP-independent mechanism to promote erythropoiesis by stimulating proliferation and differentiation of erythroid progenitors. Recombinant Human TIMP-1 is a 20.6 kDa protein containing 184 amino acid residues.

Supplier: Peprotech

Description: TIMP-2 is an extracellular inhibitor of MMPs, including MMP-1, -2, -3, -7, -8, -9, -10, -12, -13, -14, -15, -16 and -19. It belongs to the I35 (TIMP) family of irreversible protease inhibitors that function as key modulators of extracellular matrix degradation during tissue development and remodeling. TIMP-2 can also act through a MMP-independent mechanism inhibiting endothelial cell proliferation in vitro and demonstrates anti-angiogenic activities Recombinant Human TIMP-2 is a 21.8 kDa protein containing 194 amino acid residues.

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.

Catalog Number: (CA80001-988)

Supplier: MilliporeSigma

Description: Recombinant, human pro-MMP-2 expressed in mouse cells. Useful for immunoblotting, substrate cleavage and assay zymography. The ~72 kDa purified proenzyme MMP-2 may be used as a positive control or standard for zymographic analysis, immunoblotting, or substrate cleavage assays. Requires activation prior to use. 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.

Certificates

Supplier: Enzo Life Sciences

Description: MMP inhibitor

Catalog Number: (89156-472)

Supplier: Enzo Life Sciences

Description: A QuantiZymeTM 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: OmniMMPTM fluorogenic substrate Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH

Catalog Number: (10072-668)

Supplier: Prosci

Description: TIMP1 is an extracellular inhibitor of MMPs (see above) including MMP1, 2, 3, 7, 8, 9, 10, 11, 12, 13, and 16. It belongs to the I35 (TIMP) family of irreversible protease inhibitors that function as key modulators of extracellular matrix degradation during tissue development and remodeling. TIMP1 can also act through an MMP-independent mechanism to promote erythropoiesis by stimulating proliferation and differentiation of erythroid progenitors. Recombinant human TIMP-1 is a 20.6 kDa protein containing 184 amino acid residues.

Catalog Number: (89161-126)

Supplier: Enzo Life Sciences

Description: Fluorogenic substrate for ADAM8 (kcat/Km = 1.0 x 105 M-1s-1), ADAM10 (6.2 x 103), ADAM12 (2.8 x 105), TACE (TNF-α converting enzyme, ADAM17) (4.3 x 105), and likely other ADAMs, especially those that cleave TNF-α type sequences. Also efficiently cleaved by MMP-1, MMP-2, MMP-3, MMP-8, MMP-9, MMP-13, and MMP-14. FAM fluorescence is quenched by the Dabcyl group until cleavage separates them. Ex.: 485nm, Em.: 530nm. This substrate is useful for inhibitor screening and kinetic analysis.

Catalog Number: (10072-670)

Supplier: Prosci

Description: TIMP-2 is an extracellular inhibitor of MMPs including MMP1, 2, 3, 7, 8, 9, 10, 12, 13, 14, 15, 16 and 19. It belongs to the I35 (TIMP) family of irreversible protease inhibitors that function as key modulators of extracellular matrix degradation during tissue development and remodeling. TIMP-2 can also act through an MMP-independent mechanism inhibiting endothelial cell proliferation in vitro and demonstrates anti-angiogenic activities in vivo. Recombinant human TIMP-2 is a 21.8 kDa protein containing 194 amino acid residues.

Catalog Number: (89160-976)

Supplier: Enzo Life Sciences

Description: Fluorogenic substrate for TACE (ADAM17) (between Ala-Val), as well as MMP-3, MMP-7, MMP-12, and MMP-17, but not for ADAM19, MMP-13, nor MMP-14. Similar substrates are also cleaved by ADAM10, ADAM8 and ADAM9, and MMP-1, -2, and -9. This quenched substrate is useful for TACE inhibitor screening and kinetic analysis. Ex: 328 nm, Em: 393 nm, although the following Ex/Em have been used: 320-340/400-420. Also available: OMNIMMP® Fluorogenic Control peptide (BML-P127).

Supplier: Peprotech

Description: Matrix metalloproteinases (MMPs) are a family of endoproteases that require zinc and calcium for expressing catalytic activity. These enzymes play a central role in the maintenance and remodeling of the extracellular matrix. Elevated expression of their activity, caused either by up-regulation of their expression or down-regulation of their cognate inhibitors, has been implicated in various degenerative disorders, including arthritis, cardiovascular disease, skeletal growth-plate disorders, and cancer metastasis. MMP-3 degrades fibronectin, laminin, collagens III, IV, and X, and cartilage proteoglycans. Recombinant Human MMP-3 is a 42.8 kDa protein containing the entire catalytic N-terminal domain and the C-terminal domain (378 amino acids).

Catalog Number: (89358-556)

Supplier: Genetex

Description: 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. However, the enzyme encoded by this gene is activated intracellularly by furin within the constitutive secretory pathway. Also in contrast to other MMP's, this enzyme cleaves alpha 1 proteinase inhibitor but weakly degrades structural proteins of the extracellular matrix.