Millipore Sigma Vibrant Logo

PF140 MMP-9, Active, Human, Recombinant

MMP-9, Active, Human, Recombinant MSDS (material safety data sheet) or SDS, CoA and CoQ, dossiers, brochures and other available documents.

Synonyms: Gelatinase B (67 kDa), Matrix Metalloproteinase-9 (67 kDa)

View Products on Sigmaaldrich.com
PF140
View Pricing & Availability

Overview

Replacement Information

Pricing & Availability

Catalogue Number AvailabilityPackaging Qty/Pack Price Quantity
PF140-5UGCN
Retrieving availability...
—
Limited Availability Limited Availability
In Stock 
Discontinued
Limited Quantities Available
Availability to be confirmed
    Remaining : Will advise
      Remaining : Will advise
      Will advise
      Contact Customer Service
      Contact Customer Service

      		 Plastic ampoule 5 μg
      Retrieving price...
      Price could not be retrieved
      Minimum Quantity is a multiple of
      Maximum Quantity is
      Upon Order Completion More Information
      You Saved ()
       
      —
      Request Pricing
      		 —
      Description
      OverviewRecombinant, human MMP-9 with a truncated C-terminal hemopexin domain expressed as proenzyme that is activated by APMA. AMPA is removed through a Biogel-P6 column and active MMP-9 is purified.
      Catalogue NumberPF140
      Brand Family Calbiochem®
      SynonymsGelatinase B (67 kDa), Matrix Metalloproteinase-9 (67 kDa)
      References
      ReferencesParsons, 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.
      Xia, T., et al. 1996. Biochim. Biophys. 1293, 259.
      Sang, Q.X., et al. 1995. Biochim. Biophys. 1251, 99.
      Zempo, N., et al. 1994. J. Vasc. Surg. 20, 209.
      Birkedal-Hansen, H. 1993. J. Periodontol 64, 474.
      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. Cell 64, 327.
      Harris, E. 1990. N. Engl. J. Med. 322, 1277.
      Product Information
      ActivityΔA₄₀₅/h/µg protein within the range of 20.0 to 60.0 in a standard thiopeptide hydrolysis assay
      FormLiquid
      FormulationIn 50 mM Hepes, 10 mM CaCl₂, 20% glycerol, 0.005% BRIJ® 35 Detergent, pH 7.5.
      PreservativeNone
      Quality LevelMQ100
      Applications
      Application NotesImmunoblotting (1μg protein/lane)
      Zymography (0.1 μg protein/lane, see application references)
      Application CommentsThe substrate specificity for MMP-9 is collagen (types IV, V, VII, and X), elastin, and gelatin (type I).
      Biological Information
      Concentration Label Please refer to vial label for lot-specific concentration
      Physicochemical Information
      Dimensions
      Materials Information
      Toxicological Information
      Safety Information according to GHS
      Safety Information
      Product Usage Statements
      Storage and Shipping Information
      Ship Code Dry Ice Only
      Toxicity Standard Handling
      Storage ≤ -70°C
      Avoid freeze/thaw Avoid freeze/thaw
      Do not freeze Ok to freeze
      Special InstructionsFollowing initial thaw, aliquot and freeze (-70°C).
      Packaging Information
      Transport Information
      Supplemental Information
      Specifications
      Global Trade Item Number
      Catalogue Number GTIN
      PF140-5UGCN 04055977226935

      Documentation

      MMP-9, Active, Human, Recombinant SDS

      Title

      Safety Data Sheet (SDS) 

      MMP-9, Active, Human, Recombinant Certificates of Analysis

      TitleLot Number
      PF140

      References

      Reference overview
      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.
      Xia, T., et al. 1996. Biochim. Biophys. 1293, 259.
      Sang, Q.X., et al. 1995. Biochim. Biophys. 1251, 99.
      Zempo, N., et al. 1994. J. Vasc. Surg. 20, 209.
      Birkedal-Hansen, H. 1993. J. Periodontol 64, 474.
      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. Cell 64, 327.
      Harris, E. 1990. N. Engl. J. Med. 322, 1277.
      Data Sheet

      Note that this data sheet is not lot-specific and is representative of the current specifications for this product. Please consult the vial label and the certificate of analysis for information on specific lots. Also note that shipping conditions may differ from storage conditions.

      Revision18-September-2008 RFH
      SynonymsGelatinase B (67 kDa), Matrix Metalloproteinase-9 (67 kDa)
      ApplicationImmunoblotting (1μg protein/lane)
      Zymography (0.1 μg protein/lane, see application references)
      DescriptionRecombinant, human MMP-9 with a truncated C-terminal hemopexin domain expressed as proenzyme that is activated by APMA. AMPA is removed through a Biogel-P6 column and active MMP-9 is purified. The substrate specificity for MMP-9 is collagen (types IV, V, VII, and X), elastin, and gelatin (type I). 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.
      BackgroundMatrix 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.
      FormLiquid
      FormulationIn 50 mM Hepes, 10 mM CaCl₂, 20% glycerol, 0.005% BRIJ® 35 Detergent, pH 7.5.
      Concentration Label Please refer to vial label for lot-specific concentration
      Recommended reaction conditionsZymography Xia, T., et al. 1996. Biochim. Biophys. 1293, 259. Kleiner, D.E. and Stetler-Stevenson W.G. 1994. Anal. Biochem. 218, 325. Heussen, C. and Dowdle, E.B. 1980. Anal. Biochem. 102, 196. Substrate Cleavage Assay Xia, T., et al. 1996. Biochim. Biophys. 1293, 259.
      ActivityΔA₄₀₅/h/µg protein within the range of 20.0 to 60.0 in a standard thiopeptide hydrolysis assay
      PreservativeNone
      CommentsThe substrate specificity for MMP-9 is collagen (types IV, V, VII, and X), elastin, and gelatin (type I).
      Storage Avoid freeze/thaw
      ≤ -70°C
      Do Not Freeze Ok to freeze
      Special InstructionsFollowing initial thaw, aliquot and freeze (-70°C).
      Toxicity Standard Handling
      ReferencesParsons, 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.
      Xia, T., et al. 1996. Biochim. Biophys. 1293, 259.
      Sang, Q.X., et al. 1995. Biochim. Biophys. 1251, 99.
      Zempo, N., et al. 1994. J. Vasc. Surg. 20, 209.
      Birkedal-Hansen, H. 1993. J. Periodontol 64, 474.
      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. Cell 64, 327.
      Harris, E. 1990. N. Engl. J. Med. 322, 1277.