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IM64 Anti-MMP-13 (Ab-3) Mouse mAb (181-14G11)

Anti-MMP-13 (Ab-3) Mouse mAb (181-14G11) : FDS (Fiches de données de sécurité), certificats d’analyse (CoA) et de qualité (CoQ), dossiers, brochures et autres documents disponibles.

Synonymes: Anti-Collagenase-3, Anti-Matrix Metalloproteinase 13

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      Aperçu

      Replacement Information

      Tableau de caractéristiques principal

      Host
      M
      Description
      OverviewRecognizes the ~54-60 kDa latent and the ~48 kDa active forms of MMP-13.
      Catalogue NumberIM64
      Brand Family Calbiochem®
      SynonymsAnti-Collagenase-3, Anti-Matrix Metalloproteinase 13
      References
      ReferencesShlopov, B., et al. 1997. Arthritis Rheum. 40, 2065. Knauper V., et al. 1996. J. Biol. Chem. 271, 1544. Freije, J.M.P., et al. 1994. J. Biol. Chem. 269, 16766. Cottam, D. W. and Rees, R. C., 1993. Intl. J. Oncol. 2, 861. Stetler-Stevenson, et al. 1993. FASEB J. 7, 1434. Woessner, J. F., 1991. FASEB J. 5, 2145. Liotta, L. A. and Stetler-Stevenson, W. G., 1990. In Seminars in Cancer Biology, ed. M. M. Gottesman. Vol. 1, 99.
      Product Information
      DeclarationManufactured by Daiichi Fine Chemical Co., Ltd. Not available for sale in Japan.
      FormLiquid
      FormulationIn 100 mM sodium phosphate buffer, 0.1% BSA, pH 7.0
      Positive controlConditioned medium from PMA-treated HT-1080 cells or breast, bladder, or ovarian carcinoma tissue
      Preservative≤0.1% sodium azide
      Applications
      Key Applications Immunoblotting (Western Blotting)
      Paraffin Sections
      Application NotesImmunoblotting (1 µg/ml) Paraffin Sections (2.5 µg/ml)
      Application CommentsAntibody should be titrated for optimal results in individual systems.
      Biological Information
      Immunogenrecombinant human pro-MMP-13
      ImmunogenHuman
      Clone181-14G11
      HostMouse
      IsotypeIgG₁
      Physicochemical Information
      Dimensions
      Materials Information
      Toxicological Information
      Safety Information according to GHS
      Safety Information
      Product Usage Statements
      Storage and Shipping Information
      Ship Code Blue Ice Only
      Toxicity Standard Handling
      Storage -20°C
      Do not freeze Ok to freeze
      Packaging Information
      Transport Information
      Supplemental Information
      Specifications
      Global Trade Item Number
      Référence GTIN
      IM64 0

      Documentation

      Références bibliographiques

      Aperçu de la référence bibliographique
      Shlopov, B., et al. 1997. Arthritis Rheum. 40, 2065. Knauper V., et al. 1996. J. Biol. Chem. 271, 1544. Freije, J.M.P., et al. 1994. J. Biol. Chem. 269, 16766. Cottam, D. W. and Rees, R. C., 1993. Intl. J. Oncol. 2, 861. Stetler-Stevenson, et al. 1993. FASEB J. 7, 1434. Woessner, J. F., 1991. FASEB J. 5, 2145. Liotta, L. A. and Stetler-Stevenson, W. G., 1990. In Seminars in Cancer Biology, ed. M. M. Gottesman. Vol. 1, 99.
      Fiche technique

      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.

      Revision26-February-2008 JSW
      SynonymsAnti-Collagenase-3, Anti-Matrix Metalloproteinase 13
      ApplicationImmunoblotting (1 µg/ml) Paraffin Sections (2.5 µg/ml)
      DescriptionPurified mouse monoclonal antibody. Recognizes the ~54-60 kDa latent and the ~48 kDa active forms of MMP-13.
      BackgroundMatrix metalloproteinases (MMPs) are a family of enzymes that are responsible for the degradation of extracellular matrix components such as collagen, laminin and proteoglycans. In addition to sequence homology, all MMPs share the following characteristics: the catalytic mechanism is dependent upon a zinc ion at the active center, they cleave one or more extracellular matrix components, they are secreted as zymogens which are activated by removal of an approximately 10 kDa segment from the N-terminus and they are inhibited by tissue inhibitor of metalloproteinases (TIMP). These enzymes are involved in normal physiological processes such as embryogenesis and tissue remodeling and may play an important role in angiogenesis, arthritis, periodontitis, and metastasis. Matrix metalloproteinase-13 (MMP-13) also known as collagenase-3 is secreted as a 60 kDa proenzyme which is proteolytically processed to the 48 kDa active MMP-13 form. MMP-13 shows substrate specificity toward interstitial collagens I-III and gelatin, preferentially cleaving type II collagen over types I and III and cleaving fibrillar type I collagen with comparable efficiency to MMP-1 and MMP-8. MMP-13 is expressed in breast carcinomas and may be important in the turnover of articular cartilage, which is rich in type II collagen. Active MMP-13 can be inhibited in vitro by chelators of divalent ions such as EDTA and o-phenanthroline and in vivo by TIMP-1, TIMP-2, and TIMP-3. Numerous studies have shown a correlation between collagenase expression and metastatic potential and suggest that it may be a useful marker for the diagnosis or prognosis of cancer.
      HostMouse
      Immunogen speciesHuman
      Immunogenrecombinant human pro-MMP-13
      Clone181-14G11
      IsotypeIgG₁
      Specieshuman
      Positive controlConditioned medium from PMA-treated HT-1080 cells or breast, bladder, or ovarian carcinoma tissue
      FormLiquid
      FormulationIn 100 mM sodium phosphate buffer, 0.1% BSA, pH 7.0
      Preservative≤0.1% sodium azide
      CommentsAntibody should be titrated for optimal results in individual systems.
      Storage -20°C
      Do Not Freeze Ok to freeze
      Toxicity Standard Handling
      ReferencesShlopov, B., et al. 1997. Arthritis Rheum. 40, 2065. Knauper V., et al. 1996. J. Biol. Chem. 271, 1544. Freije, J.M.P., et al. 1994. J. Biol. Chem. 269, 16766. Cottam, D. W. and Rees, R. C., 1993. Intl. J. Oncol. 2, 861. Stetler-Stevenson, et al. 1993. FASEB J. 7, 1434. Woessner, J. F., 1991. FASEB J. 5, 2145. Liotta, L. A. and Stetler-Stevenson, W. G., 1990. In Seminars in Cancer Biology, ed. M. M. Gottesman. Vol. 1, 99.