475938 MT2-MMP, Catalytic Domain, Human, Recombinant, E. coli

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

Synonyms: MMP-15 Catalytic Domain

475938
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      Overview

      Replacement Information

      Key Specifications Table

      Pricing & Availability

      Catalog NumberAvailability Packaging Qty/Pack Price Quantity
      475938-10UG
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          		 Plastic ampoule 10 μg
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          Description
          OverviewRecombinant, human pro-MT2-MMP expressed in E. coli as a periplasmic protein and activated to yield the active catalytic domain (amino acids 91-267). The catalytic domain is comprised of amino acid residues Tyr91 to Gly267 of mature human MT2-MMP. MT2-MMP is used to study the activation of MMP-2 and the degradation of extracellular matrix proteins.
          Note: 1 mU = 1 milliunit.
          Catalogue Number475938
          Brand Family Calbiochem®
          SynonymsMMP-15 Catalytic Domain
          References
          ReferencesD’Ortho, M.-P., et al. 1997. Eur. J. Biochem. 250, 751.
          Kolkenbrock, H., et al. 1997. Biol. Chem. 378, 71.
          Knight, C.G., et al. 1992. FEBS Lett. 296, 263.
          Product Information
          Unit of DefinitionOne unit is defined as the amount of enzyme that will hydrolyze 1.0 µmol MCA-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH₂ (<a href ="/Products/ProductDisplay.asp→catNO=03-32-5032">Cat. No. 03-32-5032</a>) per min at 37°C, pH 7.5.
          FormLiquid
          FormulationIn 150 mM NaCl, 50 mM Tris-HCl, 5 mM CaCl₂, pH 7.5.
          Applications
          Biological Information
          Purity≥90% by SDS-PAGE
          Specific Activity≥30 mU/mg protein
          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

          Documentation

          SDS

          Title

          Safety Data Sheet (SDS) 

          Certificates of Analysis

          TitleLot Number
          475938

          References

          Reference overview
          D’Ortho, M.-P., et al. 1997. Eur. J. Biochem. 250, 751.
          Kolkenbrock, H., et al. 1997. Biol. Chem. 378, 71.
          Knight, C.G., et al. 1992. FEBS Lett. 296, 263.
          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.

          Revision17-September-2007 RFH
          SynonymsMMP-15 Catalytic Domain
          DescriptionRecombinant, human pro-MT2-MMP expressed in E. coli as a periplasmic protein and activated to yield the active catalytic domain (amino acids 91-267). The catalytic domain is comprised of amino acid residues Tyr91 to Gly267 of mature human MT2-MMP. MT2-MMP is used to study the activation of MMP-2 and the degradation of extracellular matrix proteins.
          FormLiquid
          FormulationIn 150 mM NaCl, 50 mM Tris-HCl, 5 mM CaCl₂, pH 7.5.
          Concentration Label Please refer to vial label for lot-specific concentration
          Recommended reaction conditions
          Activity Assay
          Reagent Preparation and Required Equipment Peptide Hydrolysis Buffer: 150 mM NaCl, 50 mM Tris-HCl, 5 mM CaCl2, 0.025 % Brij® 35 detergent, pH 7.5. Store at 4°C; stable for several weeks. Peptide Substrate Stock: 100 µM Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg (Cat. No. 05-32-5032) in 20% DMSO. Store at -20°C. Peptide Standard: 10 µM (7-methoxycoumarin-4-yl)acetyl-Pro-Leu-NH2 (Mca-Pro-Leu) (Cat. No. 05-32-5033) in 20% DMSO. Store at -20°C. Fluorimeter: Excitation wavelength: ~328 nm; emission wavelength: ~393 nm
          Protocol Note: This protocol is provided only as a guide; assay conditions should be optimized for individual experiments.
          The protocol is based on the following reference: Knight, C.G., et al. 1992. FEBS Lett. 296, 263.
          1. Calibrate the fluorimeter using the Peptide Standard (Mca-Pro-Leu) at a concentration that corresponds to 2–10% hydrolysis of the Peptide Substrate. 2. Kinetic Dilute the Peptide Substrate Stock to 8 µM in Peptide Hydrolysis Buffer and equilibrate to 37°C. 3. Add 2–4 µl MT2-MMP and record the increase in fluorescence at desired intervals from 2–12 min. 4. Calculate activity in units per ml enzyme using the following equation: Activity (U/ml) = cMca-Pro-Leu/FMca-Pro-Leu x ΔFMca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg/venzyme x Vtotal cMca-Pro-Leu: Concentration of Mca-Pro-Leu used for calibration of the fluorimeter (µmol/ml) FMca-Pro-Leu: Fluorescence of Mca-Pro-Leu at the concentration cMca-Pro-Leu used for fluorimeter calibration ΔFMca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg: Change in fluorescence during peptide hydrolysis per min V: Volume of peptide hydrolysis reaction (2.5 ml) v: Volume of added enzyme (2–4 µl)
          Purity≥90% by SDS-PAGE
          Specific activity≥30 mU/mg protein
          Unit definitionOne unit is defined as the amount of enzyme that will hydrolyze 1.0 µmol MCA-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH₂ (Cat. No. 03-32-5032) per min at 37°C, pH 7.5.
          Storage ≤ -70°C
          Avoid freeze/thaw
          Do Not Freeze Ok to freeze
          Special InstructionsFollowing initial thaw, aliquot and freeze (-70°C).
          Toxicity Standard Handling
          ReferencesD’Ortho, M.-P., et al. 1997. Eur. J. Biochem. 250, 751.
          Kolkenbrock, H., et al. 1997. Biol. Chem. 378, 71.
          Knight, C.G., et al. 1992. FEBS Lett. 296, 263.