444250 | MMP Inhibitor I - Calbiochem

444250
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      Overview

      Replacement Information

      Key Specifications Table

      Empirical Formula
      C₂₃H₃₄N₆O₆

      Pricing & Availability

      Catalog NumberAvailability Packaging Qty/Pack Price Quantity
      444250-10MG
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          Plastic ampoule 10 mg
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          Description
          OverviewA tetrapeptidyl hydroxamic acid that inhibits MMP-1 and MMP-8 (IC50 = 1.0 µM), MMP-9 (IC50 = 30 µM) and MMP-3 (IC50 = 150 µM). Retains its activity even after prolonged incubation with PRONASE® Protease (Cat. Nos. 53702 or 537088) or human granulocyte elastase.
          Catalogue Number444250
          Brand Family Calbiochem®
          SynonymsFN-439
          References
          ReferencesHagemamn, T., et al. 2004. Carcinogenesis 25, 1543.
          Odake, S., et al. 1994. Biochem. Biophys. Res. Commun. 199, 1442.
          Product Information
          ATP CompetitiveN
          FormWhite solid
          Hill FormulaC₂₃H₃₄N₆O₆
          Chemical formulaC₂₃H₃₄N₆O₆
          ReversibleN
          Applications
          ApplicationMMP Inhibitor I, CAS 124168-73-6, is an inhibitor of multiple MMPs (IC50 = 1.0, 1.0, 150, and 30 M for MMP-1, MMP-8, MMP-3, and MMP-9, respectively).
          Biological Information
          Primary TargetMMP-1, MMP-8
          Primary Target IC<sub>50</sub>1 µM
          Purity≥98% by HPLC
          Physicochemical Information
          Cell permeableN
          Peptide Sequence4-Abz-Gly-Pro-D-Leu-D-Ala-NH-OH [Abz = aminobenzoyl]
          Dimensions
          Materials Information
          Toxicological Information
          Safety Information according to GHS
          Safety Information
          Product Usage Statements
          Storage and Shipping Information
          Ship Code Ambient Temperature Only
          Toxicity Standard Handling
          Storage -20°C
          Do not freeze Ok to freeze
          Special InstructionsFollowing reconstitution aliquot and freeze (-20°C). Stock solutions are stable for up to 1 month at -20°C.
          Packaging Information
          Transport Information
          Supplemental Information
          Specifications

          Documentation

          SDS

          Title

          Safety Data Sheet (SDS) 

          Certificates of Analysis

          TitleLot Number
          444250

          References

          Reference overview
          Hagemamn, T., et al. 2004. Carcinogenesis 25, 1543.
          Odake, S., et al. 1994. Biochem. Biophys. Res. Commun. 199, 1442.

          Citations

          Title
        • Anthony R. White, et al. (2006) Degradation of the alzheimer disease amyloid -peptide by metal-dependent up-regulation of metalloprotease activity. journal of Biological Chemistry 281, 17670-17680.
        • 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.

          Revision06-August-2008 RFH
          SynonymsFN-439
          DescriptionA tetrapeptidyl hydroxamic acid that inhibits interstitial and granulocyte collagenases (MMP-1 and MMP-8; IC50 = 1 µM), granulocyte gelatinase (MMP-9; IC50 = 30 µM), adn skin fibroblast stromelysin (MMP-3; IC50 = 150 µM). Retains its activity even after prolonged incubation with PRONASE® Protease (Cat. No. 53702) or human neutrophil elastase.
          FormWhite solid
          Chemical formulaC₂₃H₃₄N₆O₆
          Peptide Sequence4-Abz-Gly-Pro-D-Leu-D-Ala-NH-OH [Abz = aminobenzoyl]
          Purity≥98% by HPLC
          SolubilityH₂O (1 mg/ml)
          Storage -20°C
          Do Not Freeze Ok to freeze
          Special InstructionsFollowing reconstitution aliquot and freeze (-20°C). Stock solutions are stable for up to 1 month at -20°C.
          Toxicity Standard Handling
          ReferencesHagemamn, T., et al. 2004. Carcinogenesis 25, 1543.
          Odake, S., et al. 1994. Biochem. Biophys. Res. Commun. 199, 1442.
          Citation
        • Anthony R. White, et al. (2006) Degradation of the alzheimer disease amyloid -peptide by metal-dependent up-regulation of metalloprotease activity. journal of Biological Chemistry 281, 17670-17680.