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PF023 MMP-2, Active, Human, Recombinant, Mouse Cells

MMP-2, Active, Human, Recombinant, Mouse Cells MSDS (material safety data sheet) or SDS, CoA and CoQ, dossiers, brochures and other available documents.

Synonyms: Gelatinase A, Active Matrix Metalloproteinase 2

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PF023
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PF023-5UG
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      Description
      OverviewFull-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.
      Catalogue NumberPF023
      Brand Family Calbiochem®
      SynonymsGelatinase A, Active Matrix Metalloproteinase 2
      References
      ReferencesLiepnisch, E., et al. 2003. J. Biol. Chem. 278, 25982.
      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. Acta 1293, 259.
      Chandler, S., et al. 1995 Neuroscience Letters 201, 226.
      Sang, Q.X., et al. 1995. Biochim. Biophys. Acta 1251, 99.
      Kenagy, R.D. and Clowes, A.W. 1994. In Inhibition of Matrix Metalloproteinases: Therapeutic Potential. Greenwald, R.A. and Golub L.M., Eds, 465.
      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.
      Delaisse, J-M. and Vaes, G. 1992. In Biology and Physiology of the Osteoclast. B.R. Rifkin and C.V. Gay, Eds., 290.
      Jeffrey, J.J. 1992. In Wound Healing: Biochemical and Clinical Aspects. R.F. Diegelmann and W.J. Lindblad, Eds., 194.
      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
      ActivityΔΑ₄₀₅/hour/µg protein: ≥ 7.0 in standard thiopeptolide hydrolysis assays.
      EC number3.4.24.24
      FormLiquid
      FormulationIn 50 mM HEPES, 10 mM CaCl₂, 20% glycerol, 0.005% BRIJ®-35 Detergent, pH 7.5.
      PreservativeNone
      Quality LevelMQ100
      Applications
      Biological Information
      Purity≥90% by SDS-PAGE; contains 9% TIMP-2
      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 use, aliquot into siliconized vials and freeze (-70°C).
      Packaging Information
      Transport Information
      Supplemental Information
      Specifications
      Global Trade Item Number
      Catalogue Number GTIN
      PF023-5UG 04055977207958

      Documentation

      MMP-2, Active, Human, Recombinant, Mouse Cells MSDS

      Title

      Safety Data Sheet (SDS) 

      MMP-2, Active, Human, Recombinant, Mouse Cells Certificates of Analysis

      TitleLot Number
      PF023

      References

      Reference overview
      Liepnisch, E., et al. 2003. J. Biol. Chem. 278, 25982.
      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. Acta 1293, 259.
      Chandler, S., et al. 1995 Neuroscience Letters 201, 226.
      Sang, Q.X., et al. 1995. Biochim. Biophys. Acta 1251, 99.
      Kenagy, R.D. and Clowes, A.W. 1994. In Inhibition of Matrix Metalloproteinases: Therapeutic Potential. Greenwald, R.A. and Golub L.M., Eds, 465.
      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.
      Delaisse, J-M. and Vaes, G. 1992. In Biology and Physiology of the Osteoclast. B.R. Rifkin and C.V. Gay, Eds., 290.
      Jeffrey, J.J. 1992. In Wound Healing: Biochemical and Clinical Aspects. R.F. Diegelmann and W.J. Lindblad, Eds., 194.
      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.

      Brochure

      Title
      Art of Metastasis Poster PDF ( 610 KB )

      Citations

      Title
    • Kan V. Lu, et al. (2004) Upregulation of tissue inhibitor of metalloproteinases (TIMP)-2 promotes matrix metalloproteinase (MMP)-2 activation and cell invasion in a human glioblastoma cell line. Laboratory Investigation 84, 8-20.
      		•
      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.

      Revision21-September-2017 JSW
      SynonymsGelatinase A, Active Matrix Metalloproteinase 2
      DescriptionFull-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.
      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 conditions
      Zymography Xia, T., et al. 1996. Biochim. Biophys. Acta 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. Acta 1293, 259.
      EC number3.4.24.24
      Purity≥90% by SDS-PAGE; contains 9% TIMP-2
      ActivityΔΑ₄₀₅/hour/µg protein: ≥ 7.0 in standard thiopeptolide hydrolysis assays.
      PreservativeNone
      Storage Avoid freeze/thaw
      ≤ -70°C
      Do Not Freeze Ok to freeze
      Special InstructionsFollowing initial use, aliquot into siliconized vials and freeze (-70°C).
      Toxicity Standard Handling
      ReferencesLiepnisch, E., et al. 2003. J. Biol. Chem. 278, 25982.
      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. Acta 1293, 259.
      Chandler, S., et al. 1995 Neuroscience Letters 201, 226.
      Sang, Q.X., et al. 1995. Biochim. Biophys. Acta 1251, 99.
      Kenagy, R.D. and Clowes, A.W. 1994. In Inhibition of Matrix Metalloproteinases: Therapeutic Potential. Greenwald, R.A. and Golub L.M., Eds, 465.
      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.
      Delaisse, J-M. and Vaes, G. 1992. In Biology and Physiology of the Osteoclast. B.R. Rifkin and C.V. Gay, Eds., 290.
      Jeffrey, J.J. 1992. In Wound Healing: Biochemical and Clinical Aspects. R.F. Diegelmann and W.J. Lindblad, Eds., 194.
      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.
      Citation
    • Kan V. Lu, et al. (2004) Upregulation of tissue inhibitor of metalloproteinases (TIMP)-2 promotes matrix metalloproteinase (MMP)-2 activation and cell invasion in a human glioblastoma cell line. Laboratory Investigation 84, 8-20.
      		•