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Metalloproteinases and Proteases

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MMPs & proteases involved in ECM layer degradation.
Merck Millipore offers a full range of MMP antibodies, proteins, and activity assays for interrogating the function and regulation of metalloproteinases (MMPs) in both normal and disease states.

Matrix metalloproteinases (MMPs) are secreted or transmembrane proteolytic endopeptidases that process and degrade extracellular matrix proteins. MMPs play critical roles in many normal growth and developmental aspects of tissue remodeling, wound healing, and angiogenesis. In a pathological context, MMPs are associated with cell migration, invasion, arthritis, and cancer tumor progression. Once activated, the MMPs are subject to inhibition by the tissue inhibitors of metalloproteinases (TIMPs) that bind MMPs non-covalently. ADAMs (A Disintegrin And Metalloprotease protein) are members of the same superfamily as MMPs and are cell surface proteins that possess both an adhesion domain as well as a protease domain.
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PRODUCT HIGHLIGHT
MMP-2 Proform, N-terminus, clone CA-4001 Antibody
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.
Staining of paraformaldehye-fixed piglet intestine, using Anti-MMP-2 Profrom , clone CA-4001 and a fluorescent labeled goat anti-mouse IgG. The tissue was counterstained with Propidium Iodide (red). The green represents the MMP specific regions, and the yellow represents dual labeling with PI and fluorescence overlap. Photo courtesy of Dr. Doug Burrin. 
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. MMPs have a common mode of activation, a conserved amino acid sequence in the putative metal binding-active site region, and are inhibited by specific tissue inhibitors of metalloproteinases (TIMPs). 

This antibody recognizes the pro (latent) of matrix metalloproteinase-2 and any fragment with N-terminal (proform) domain still attached. Antibody shows no cross-reaction with pro and active forms of MMP-9. This antibody cross-reacts with human, mouse and rat species and has been validated in western blot, immunohistochemistry, immunofluorescence and has been shown to functionally block MMP-2 activity.

PRODUCT HIGHLIGHT
GM6001 MMP Inhibitor
GM6001 inhibits MMP-2 activity at concentrations greater than 0.1nM.
GM6001 inhibits MMP-2 activity at concentrations greater than 0.1nM
GM6001 (Ilomastat, Galardin, N-[(2R)-2-(hydroxamidocarbonylmethyl)-4-methylpentanoyl]-L-tryptophan methylamide) is a potent broad-spectrum hydroxamate inhibitor of matrix metalloproteinases (MMPs) and collagenases that can be used in both in vitro and in vivo applications to assess the biological effects of perturbing MMP activity. GM6001 pan-MMP inhibitor is available in 1 mg (Cat. No. CC1000), 10 mg (Cat. No. CC1010) & 100 mg (Cat. No. CC1100) quantities.