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538540 MMP-7, Proenzyme, Human, Recombinant, E. coli

MSDS (material safety data sheet) or SDS, CoA and CoQ, dossiers, brochures and other available documents.

Synonyms: Promatrilysin, rhPro-MMP-7

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538540
  
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      Overview

      Replacement Information
      Description
      OverviewRecombinant, human pro-MMP-7 expressed in E. coli. MMP-7 is believed to be a key factor in the regulation of metastasis. Overexpression of MMP-7 is observed in colon cancer. Activatable by organomercurials (APMA; Cat. No. 164610).
      Catalogue Number538540
      Brand Family Calbiochem®
      SynonymsPromatrilysin, rhPro-MMP-7
      References
      ReferencesGirolamo, N. D., et al. 2001. Invest. Ophtal. Visual. Sci. 42, 1963.
      Kihira, Y., et al. 1996. Urol. Oncol. 2, 20.
      Woessner, J.F. 1995. Methods Enzymol. 248, 485.
      Crabbe, T., et al. 1992. Biochemistry 31, 8500.
      Product Information
      Unit of DefinitionOne unit is defined as the amount of enzyme that will digest 1.0 µg AZOCOLL™ Substrate (Cat. No. 194933), in the presence of 500 μM <i>p</i>-aminophenylmercuric acetate (APMA; Cat. No. 164610) per minute at 37°C, pH 7.5.
      EC number3.4.24.23
      FormLiquid
      FormulationIn 150 mM NaCl, 25 mM Tris-HCl, 5 mM CaCl₂, 0.02% NaN₃, 0.01% BRIJ® 35 Detergent, pH 7.5.
      Quality LevelMQ100
      Applications
      Biological Information
      Specific Activity≥1400 units/mg protein (after activation)
      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). Freeze-thaw cycles may accelerate the activation process.
      Packaging Information
      Transport Information
      Supplemental Information
      Specifications
      Global Trade Item Number
      Catalog Number GTIN
      538540 0

      Documentation

      MMP-7, Proenzyme, Human, Recombinant, E. coli SDS

      Title

      Safety Data Sheet (SDS) 

      MMP-7, Proenzyme, Human, Recombinant, E. coli Certificates of Analysis

      TitleLot Number
      538540

      References

      Reference overview
      Girolamo, N. D., et al. 2001. Invest. Ophtal. Visual. Sci. 42, 1963.
      Kihira, Y., et al. 1996. Urol. Oncol. 2, 20.
      Woessner, J.F. 1995. Methods Enzymol. 248, 485.
      Crabbe, T., et al. 1992. Biochemistry 31, 8500.
      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-July-2007 RFH
      SynonymsPromatrilysin, rhPro-MMP-7
      DescriptionRecombinant, human pro-MMP-7 expressed in E. coli. MMP-7 is believed to be a key factor in the regulation of metastasis. Overexpression of MMP-7 is observed in colon cancer. Activatable by organomercurials (APMA; Cat. No. 164610).
      FormLiquid
      FormulationIn 150 mM NaCl, 25 mM Tris-HCl, 5 mM CaCl₂, 0.02% NaN₃, 0.01% BRIJ® 35 Detergent, pH 7.5.
      Concentration Label Please refer to vial label for lot-specific concentration
      Recommended reaction conditions

      Organomercurial Activation Protocol This protocol is provided only as a general guide. Researchers should standardize this assay for their own specific needs and should consult published literature. The following protocol is from Stricklin, et al., which describes the use of p-aminophenylmercuric acetate (APMA) to activate pro-MMP. This protocol is also adaptable to other types of organomercurals, such as p-(hydroxymercuric) benzoate (PHMB), phenylmercuric chloride (PMC), or mersalyl. 1. Prepare a 10-50 mM stock solution of APMA (or other organomercurial compound) in 0.1 M NaOH just prior to use. Although not absolutely necessary, the stock solution may be adjusted to pH 11 with 5 N HCl (see Marcy, A.I., et al.). 2. To initiate the activation mix the proenzyme solution with the APMA solution at a 10:1 volume ratio (MMP:APMA). If a higher concentration of APMA is desired, increase the concentration of the stock solution. Do not exceed the 10:1 ratio, as this could result in significant changes in pH. 3. Incubate the mixture at 37°C for 2-3 h. It is recommended that an analytical run be conducted first to determine the optimal incubation time. For example, a small-scale experiment with a fixed concentration of pro-MMP and organomercurial would be incubated as described above. Remove aliquots of the sample at various time points during the incubation. Stop the reaction by the addition of SDS-PAGE sample buffer (e.g., 10 µl 2X sample buffer to 10 µl aliquot) and heat the samples to 95°C. The progress of activation can be monitored qualitatively by analyzing the aliquots on a 12% SDS-PAGE gel. 4. The activated MMP can be used without removing the APMA from the mixture. Please refer to Marcy, A.I., et al. for removal of organomercurials by gel filtration.
      EC number3.4.24.23
      Specific activity≥1400 units/mg protein (after activation)
      Unit definitionOne unit is defined as the amount of enzyme that will digest 1.0 µg AZOCOLL™ Substrate (Cat. No. 194933), in the presence of 500 μM p-aminophenylmercuric acetate (APMA; Cat. No. 164610) per minute at 37°C, pH 7.5.
      Storage Avoid freeze/thaw
      ≤ -70°C
      Do Not Freeze Ok to freeze
      Special InstructionsFollowing initial thaw, aliquot and freeze (-70°C). Freeze-thaw cycles may accelerate the activation process.
      Toxicity Standard Handling
      ReferencesGirolamo, N. D., et al. 2001. Invest. Ophtal. Visual. Sci. 42, 1963.
      Kihira, Y., et al. 1996. Urol. Oncol. 2, 20.
      Woessner, J.F. 1995. Methods Enzymol. 248, 485.
      Crabbe, T., et al. 1992. Biochemistry 31, 8500.

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