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PC311 Anti-MMP-1 (Ab-3) Sheep pAb

Anti-MMP-1 (Ab-3) Sheep pAb MSDS (material safety data sheet) or SDS, CoA and CoQ, dossiers, brochures and other available documents.
PC311
  
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      Overview

      Replacement Information

      Key Spec Table

      Host
      Sh
      Description
      Overview

      This product has been discontinued.





      Recognizes the ~55 kDa latent and the ~43 kDa active forms of MMP-1 in PMA-treated HT1080 cells. In some cell lines, (i.e. stimulated, connective tissue cells) a minor glycosylated form of MMP-1 may be seen as a doublet of 55-57 kDa.
      Catalogue NumberPC311
      Brand Family Calbiochem®
      References
      ReferencesCottam, D.W. and Rees, R.C. 1993. Intl. J. Oncol. 2, 861.
      Stetler-Stevenson, W.G., 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
      FormLiquid
      FormulationIn phosphate buffer, 0.2% BSA.
      Positive controlConditioned medium from PMA-treated HT-1080 cells
      Preservative≤0.1% sodium azide
      Applications
      Key Applications Immunoblotting (Western Blotting)
      Application NotesImmunoblotting (1:150)
      Application CommentsIn some cell lines (i.e. stimulated connective tissue cells), a minor glycosylated form of MMP-1 may be seen as a doublet of ~55-57 kDa in SDS-PAGE. For immunoblotting, the suggested dilution is 1:150 to detect 50 ng/lane of MMP-1. To prepare conditioned medium for positive control, incubate HT1080 cells with serum free media containing 100 nM of PMA for 2 h at 37°C. Collect and centrifuge medium; concentrate if necessary. Store conditioned media in aliquots at -20°C. Antibody should be titrated for optimal results in individual systems.
      Biological Information
      Immunogenpurified, human breast carcinoma pro-MMP-1
      ImmunogenHuman
      HostSheep
      IsotypeIgG
      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 -20°C
      Avoid freeze/thaw Avoid freeze/thaw
      Do not freeze Ok to freeze
      Special InstructionsFollowing initial thaw, aliquot and freeze (-20°C).
      Packaging Information
      Transport Information
      Supplemental Information
      Specifications
      Global Trade Item Number
      Catalogue Number GTIN
      PC311 0

      Documentation

      Anti-MMP-1 (Ab-3) Sheep pAb Certificates of Analysis

      TitleLot Number
      PC311

      References

      Reference overview
      Cottam, D.W. and Rees, R.C. 1993. Intl. J. Oncol. 2, 861.
      Stetler-Stevenson, W.G., 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.
      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.

      Revision09-October-2007 RFH
      ApplicationImmunoblotting (1:150)
      DescriptionPurified sheep polyclonal antibody. Recognizes the ~55 kDa latent and the ~43 kDa active forms of MMP-1.
      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 ~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. MMP-1 (interstitial collagenase, tissue collagenase, fibroblast collagenase) is secreted as a 57/52 kDa zymogen which is proteolytically processed to the 46/42 kDa active forms. This enzyme displays substrate specificity toward type I, II, III, VII, VIII and X collagens and gelatin. MMP-1 is thought to play an important role in pathophysiological degradation processes associated with conditions such as rheumatoid arthritis, osteoarthritis and cancer cell invasion.
      HostSheep
      Immunogen speciesHuman
      Immunogenpurified, human breast carcinoma pro-MMP-1
      IsotypeIgG
      Specieshuman
      Positive controlConditioned medium from PMA-treated HT-1080 cells
      FormLiquid
      FormulationIn phosphate buffer, 0.2% BSA.
      Concentration Label Please refer to vial label for lot-specific concentration
      Preservative≤0.1% sodium azide
      CommentsIn some cell lines (i.e. stimulated connective tissue cells), a minor glycosylated form of MMP-1 may be seen as a doublet of ~55-57 kDa in SDS-PAGE. For immunoblotting, the suggested dilution is 1:150 to detect 50 ng/lane of MMP-1. To prepare conditioned medium for positive control, incubate HT1080 cells with serum free media containing 100 nM of PMA for 2 h at 37°C. Collect and centrifuge medium; concentrate if necessary. Store conditioned media in aliquots at -20°C. Antibody should be titrated for optimal results in individual systems.
      Storage Avoid freeze/thaw
      -20°C
      Do Not Freeze Ok to freeze
      Special InstructionsFollowing initial thaw, aliquot and freeze (-20°C).
      Toxicity Standard Handling
      ReferencesCottam, D.W. and Rees, R.C. 1993. Intl. J. Oncol. 2, 861.
      Stetler-Stevenson, W.G., 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.