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AnaSpec Introduces new MMP Recombinant Proteins
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AnaSpec has announced the release of three new MMP recombinant proteins, MMP-1, MMP-9 and MMP-12. These proteins, derived from the catalytic domain of the proteins, are supplied as activated proteins (activation by APMA is not necessary). They can be used as positive controls for the SensoLyte® 520 and 490 assays, for western blot, immunoprecipitation, ELISA or zymography.
Matrix metalloproteinases (MMPs) belong to a family of secreted or membrane-associated zinc endopeptidases capable of digesting extracellular matrix components. MMP-1 (collagenase-1) is involved in tumor development, metastasis and rheumatoid arthritis. MMP-1 is proposed as a therapeutic target for these diseases. It digests a broad range of substrates, including a-1 antitrypsin, myelin basic protein, collagen I, II, III, VII, VIII, casein, gelatin, and others.
MMP-9 (92-kDa gelatinase, collagenase-IV) is involved in a number of diseases such as cancer, angiogenesis, alopecia, and metastasis. MMP-9 is secreted as zymogen with prodomain, gelatin-binding domain consisting of three contiguous fibronectin type II units, catalytic domain, proline-rich linker region, and C-terminal hemopexin-like domain. It can degrade a variety of substrates, including gelatin, collagens type IV, V, XIV, a2-macroglobulin, elastin, vitronectin, and proteoglycans.
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 a-1 proteinase inhibitor, a-2 antiplasmin, plasminogen activator inhibitor-2, collagen IV, laminin, fibronectin, elastin, but not interstitial collagens.
Matrix metalloproteinases (MMPs) belong to a family of secreted or membrane-associated zinc endopeptidases capable of digesting extracellular matrix components. MMP-1 (collagenase-1) is involved in tumor development, metastasis and rheumatoid arthritis. MMP-1 is proposed as a therapeutic target for these diseases. It digests a broad range of substrates, including a-1 antitrypsin, myelin basic protein, collagen I, II, III, VII, VIII, casein, gelatin, and others.
MMP-9 (92-kDa gelatinase, collagenase-IV) is involved in a number of diseases such as cancer, angiogenesis, alopecia, and metastasis. MMP-9 is secreted as zymogen with prodomain, gelatin-binding domain consisting of three contiguous fibronectin type II units, catalytic domain, proline-rich linker region, and C-terminal hemopexin-like domain. It can degrade a variety of substrates, including gelatin, collagens type IV, V, XIV, a2-macroglobulin, elastin, vitronectin, and proteoglycans.
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 a-1 proteinase inhibitor, a-2 antiplasmin, plasminogen activator inhibitor-2, collagen IV, laminin, fibronectin, elastin, but not interstitial collagens.
