444287 | MMP-13, Human, Recombinant, Active

444287
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      Overview

      Replacement Information

      Key Specifications Table

      Pricing & Availability

      Catalog NumberAvailability Packaging Qty/Pack Price Quantity
      444287-5UG
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      Discontinued
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          Plastic ampoule 5 μg
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          Description
          OverviewRecombinant, human MMP-13. MMP-13 is a collagenase-3 enzyme that degrades a range of extracellular matrix proteins, including collagen types I, II, III, IV, IX, X, and XIV, gelatin, aggrecan, perlecan and fibronectin. It is distinguished from other human collagenases by the fact that it effectively degrades type II collagen. The importance of MMP-13 is further strengthened by reports that it is a biomarker for poor prognosis in many carcinomas and other type of cancers.
          Catalogue Number444287
          Brand Family Calbiochem®
          References
          ReferencesFreije, M.P.S., et al. 1994. J. Biol. Chem. 269,16766.
          Product Information
          Unit of DefinitionOne unit is defined as the amount of APMA-activated enzyme that will hydrolyze 1µmol MCA-Pro-Leu-Lys-Gly-Leu-DPA-Ala-Arg-NH₂ (Cat. No. 03-32-5032) at 37°C, pH 7.5.
          FormLiquid
          FormulationIn 50 mM HEPES, 10 mM CaCl₂, 20% glycerol, 0.005% BRIJ® 35 Detergent, pH 7.5. APMA-free.
          Applications
          Biological Information
          Specific Activity≥50 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
          444287

          References

          Reference overview
          Freije, M.P.S., et al. 1994. J. Biol. Chem. 269,16766.

          Brochure

          Title
          Biologics 32.4 ( 1.19 MB )
          Calbiochem Biologics 32.2
          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.

          Revision05-March-2009 JSW
          DescriptionRecombinant, human MMP-13. MMP-13 is a collagenase-3 enzyme that degrades a range of extracellular matrix proteins, including collagen types I, II, III, IV, IX, X, and XIV, gelatin, aggrecan, perlecan and fibronectin. It is distinguished from other human collagenases by the fact that it effectively degrades type II collagen. The importance of MMP-13 is further strengthened by reports that it is a biomarker for poor prognosis in many carcinomas and other type of cancers.
          FormLiquid
          FormulationIn 50 mM HEPES, 10 mM CaCl₂, 20% glycerol, 0.005% BRIJ® 35 Detergent, pH 7.5. APMA-free.
          Concentration Label Please refer to vial label for lot-specific concentration
          Specific activity≥50 mU/mg protein
          Unit definitionOne unit is defined as the amount of APMA-activated enzyme that will hydrolyze 1µmol MCA-Pro-Leu-Lys-Gly-Leu-DPA-Ala-Arg-NH₂ (Cat. No. 03-32-5032) 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
          ReferencesFreije, M.P.S., et al. 1994. J. Biol. Chem. 269,16766.