PF024
MMP-9, Active, Human, Recombinant
Synonyme(s) :
Gelatinase B, 83 kDa Gelatinase, Matrix Metalloproteinase 9, Matrix Metalloproteinase 9, Gelatinase B, 83 kDa Gelatinase
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About This Item
Pureté
≥90% (SDS-PAGE)
Niveau de qualité
Forme
liquid
Activité spécifique
≥8.0 ΔA405/h-μg protein (thiopeptide hydrolysis assay)
Ne contient pas
preservative
Fabricant/nom de marque
Calbiochem®
Conditions de stockage
OK to freeze
avoid repeated freeze/thaw cycles
Conditions d'expédition
wet ice
Température de stockage
−70°C
Description générale
Recombinant, human MMP-9 purified from transfected mammalian cells and activated with APMA. Active MMP-9 enzyme is APMA-free.
Recombinant, human MMP-9 purified from transfected mammalian cells and activated with APMA. Active MMP-9 enzyme is APMA-free. Supplied as the ~83 kDa active enzyme. The proenzyme form of MMP-9 was purified from transfected mammalian cells and activated using the organomercurial compound, 4-aminophenyl mercuric acetate (APMA). APMA is removed through a desalting column. The substrate specificity for MMP-9 is collagen (types IV, V, VII, and X), elastin, and gelatin (type I). Useful for immunoblotting, substrate cleavage, and zymography. Titration is recommended for optimal results in individual systems. 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.
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.
Conditionnement
Please refer to vial label for lot-specific concentration.
Avertissement
Toxicity: Standard Handling (A)
Forme physique
In 50 mM HEPES, 10 mM CaCl₂, 20% glycerol, 0.005% BRIJ®-35 Detergent, pH 7.5.
Reconstitution
Following initial use, aliquot into siliconized vials and freeze (-70°C).
Autres remarques
Parsons, S.L., et al. 1997. Br. J. Surg.84, 160.
Backstrom, J.R., et al. 1996. J. Neuro.16, 7910.
Lim, G.P., et al. 1996. J. Neurochem.67, 251.
Xia, T., et al. 1996. Biochim. Biophys. Acta1293, 259.
Sang, Q.X., et al. 1995. Biochim. Biophys. Acta1251, 99.
Zempo, N., et al. 1994. J. Vasc. Surg.20, 217.
Birkedal-Hansen, H. 1993. J. Periodontol.64, 484.
Stetler-Stevenson, W.G., et al. 1993. FASEB J.7, 1434.
Jeffrey, J.J. 1991. Semin. Perinatol.15, 118.
Liotta, L.A., et al. 1991. Cell64, 327.
Harris, E. 1990. N. Engl. J. Med.322, 1277.
Backstrom, J.R., et al. 1996. J. Neuro.16, 7910.
Lim, G.P., et al. 1996. J. Neurochem.67, 251.
Xia, T., et al. 1996. Biochim. Biophys. Acta1293, 259.
Sang, Q.X., et al. 1995. Biochim. Biophys. Acta1251, 99.
Zempo, N., et al. 1994. J. Vasc. Surg.20, 217.
Birkedal-Hansen, H. 1993. J. Periodontol.64, 484.
Stetler-Stevenson, W.G., et al. 1993. FASEB J.7, 1434.
Jeffrey, J.J. 1991. Semin. Perinatol.15, 118.
Liotta, L.A., et al. 1991. Cell64, 327.
Harris, E. 1990. N. Engl. J. Med.322, 1277.
Informations légales
Brij is a registered trademark of Croda International PLC
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
Code de la classe de stockage
10 - Combustible liquids
Classe de danger pour l'eau (WGK)
WGK 1
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
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