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IM61 Anti-MMP-9 (Ab-7) Mouse mAb (GE-213)

Anti-MMP-9 (Ab-7) Mouse mAb (GE-213) MSDS (material safety data sheet) or SDS, CoA and CoQ, dossiers, brochures and other available documents.

Synonyms: Anti-Type IV Collagenase, Anti-Gelatinase B, Anti-92 kDa Gelatinase, Anti-Matrix Metalloproteinase 9

IM61
  
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      Overview

      Replacement Information

      Key Spec Table

      Host
      M
      Description
      Overview

      This product has been discontinued.





      Recognizes the ~92 kDa latent and the ~78 kDa active forms of MMP-9 in dexamethasone-treated HT1080 cells, HUVEC, and breast carcinoma tissue. Also recognizes the ~200 kDa MMP-9/TIMP-1 complex. Does not cross-react with MMP-2.
      Catalogue NumberIM61
      Brand Family Calbiochem®
      SynonymsAnti-Type IV Collagenase, Anti-Gelatinase B, Anti-92 kDa Gelatinase, Anti-Matrix Metalloproteinase 9
      Application Data
      Detection of human MMP-9 by immunoprecipitation. Sample: Human MMP-9. Primary antibody: Anti-MMP-9 (Ab-7) Mouse mAb (GE-213) (Cat. No. IM61) (assay dependent). Detection: chemiluminescence.
      References
      ReferencesNikkari, S.T., et al. 1996. Amer. J. Pathol. 149, 1427.
      Visscher, D.W., et al. 1994. Intl. J. Cancer 59, 339.
      Cottam, D.W. and Rees, R.C. 1993. Intl. J. Oncol. 2, 861.
      Schnaper, H.W., et al. 1993. J. Cell. Physiol. 156, 235.
      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
      DeclarationNot available for sale in Japan.
      FormLiquid
      FormulationIn 10 mM PBS, 0.2% BSA, pH 7.4.
      Positive controlConditioned serum-free medium from dexamethasone-treated HT-1080 or HUVEC cells or breast carcinoma tissue
      Preservative≤0.1% sodium azide
      Applications
      Application ReferencesOriginal Clone Hurskainen, T., et al. 1996. J. Histochem. Cytochem. 44, 1379. Soini, Y., et al. 1994. J. Histochem. Cytochem. 42, 945.
      Key Applications Frozen Sections
      Immunoprecipitation
      Application NotesFrozen Sections (1:100)
      Immunoprecipitation (10 µl/mg protein lysate)
      Application CommentsPositive controls include cytotrophoblastic columns, endothelial and fibroblastic stromal cells of villi, and the large decidual membrane in placenta, macrophages in arteries and fibroblast, endothelial and tumor cells in breast carcinomas as well as conditioned serum free medium from dexamethasone-treated HT1080 or HUVEC cells. Antibody should be titrated for optimal results in individual systems.
      Biological Information
      Immunogenpurified, human MMP-9
      ImmunogenHuman
      CloneGE-213
      HostMouse
      IsotypeIgG₁
      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 Blue Ice Only
      Toxicity Standard Handling
      Storage +2°C to +8°C
      Avoid freeze/thaw Avoid freeze/thaw
      Do not freeze Ok to freeze
      Special InstructionsFor long-term storage, aliquot and freeze (-20°C). Avoid freeze/thaw cycles.
      Packaging Information
      Transport Information
      Supplemental Information
      Specifications
      Global Trade Item Number
      Catalogue Number GTIN
      IM61 0

      Documentation

      Anti-MMP-9 (Ab-7) Mouse mAb (GE-213) Certificates of Analysis

      TitleLot Number
      IM61

      References

      Reference overview
      Nikkari, S.T., et al. 1996. Amer. J. Pathol. 149, 1427.
      Visscher, D.W., et al. 1994. Intl. J. Cancer 59, 339.
      Cottam, D.W. and Rees, R.C. 1993. Intl. J. Oncol. 2, 861.
      Schnaper, H.W., et al. 1993. J. Cell. Physiol. 156, 235.
      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.

      Revision14-April-2009 RFH
      SynonymsAnti-Type IV Collagenase, Anti-Gelatinase B, Anti-92 kDa Gelatinase, Anti-Matrix Metalloproteinase 9
      ApplicationFrozen Sections (1:100)
      Immunoprecipitation (10 µl/mg protein lysate)
      Application Data
      Detection of human MMP-9 by immunoprecipitation. Sample: Human MMP-9. Primary antibody: Anti-MMP-9 (Ab-7) Mouse mAb (GE-213) (Cat. No. IM61) (assay dependent). Detection: chemiluminescence.
      DescriptionPurified mouse monoclonal antibody generated by immunizing BALB/c mice with purified the specified immunogen and fusing the splenocytes with mouse myeloma p3-X63-Ag8.653 cells (see application references). Recognizes the ~92 kDa latent and the ~78 kDa active forms of MMP-9 and the ~200 kDa MMP-9/TIMP-1 complex.
      BackgroundMatrix metalloproteinases (MMP's) 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 MMP's 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). MMP-9 also known as gelatinase B, 92 kDa gelatinase/type IV collagenase (EC 3.4.24.35) has a broad range of substrate specificity for native collagens including types IV, V, VII and X as well as gelatin, proteoglycans and elastin. MMP-9 is secreted as a 92 kDa proenzyme and can be activated in vitro by organomercurials (e.g., 4-aminophenylmercuric acetate, APMA), trypsin, and α-chymotrypsin and in vivo by cathepsin G and MMP-3 to the 83 kDa active form. The activity of MMP-9 can be inhibited by TIMPs in a 1:1 molar ratio. TIMP-1 is known to bind exclusively to pro-MMP-9 (Kd approximately 35 nM) whereas TIMP-2 binds to pro-MMP-2 with a Kd approximately 5 nM. MMP-9 has been measured in human plasma from normal individuals and has been shown to be elevated in sera of patients with hepatocellular carcinomas.
      HostMouse
      Immunogen speciesHuman
      Immunogenpurified, human MMP-9
      CloneGE-213
      IsotypeIgG₁
      Specieshuman
      Positive controlConditioned serum-free medium from dexamethasone-treated HT-1080 or HUVEC cells or breast carcinoma tissue
      FormLiquid
      FormulationIn 10 mM PBS, 0.2% BSA, pH 7.4.
      Concentration Label Please refer to vial label for lot-specific concentration
      Preservative≤0.1% sodium azide
      CommentsPositive controls include cytotrophoblastic columns, endothelial and fibroblastic stromal cells of villi, and the large decidual membrane in placenta, macrophages in arteries and fibroblast, endothelial and tumor cells in breast carcinomas as well as conditioned serum free medium from dexamethasone-treated HT1080 or HUVEC cells. Antibody should be titrated for optimal results in individual systems.
      Storage Avoid freeze/thaw
      +2°C to +8°C
      Do Not Freeze Ok to freeze
      Special InstructionsFor long-term storage, aliquot and freeze (-20°C). Avoid freeze/thaw cycles.
      Toxicity Standard Handling
      ReferencesNikkari, S.T., et al. 1996. Amer. J. Pathol. 149, 1427.
      Visscher, D.W., et al. 1994. Intl. J. Cancer 59, 339.
      Cottam, D.W. and Rees, R.C. 1993. Intl. J. Oncol. 2, 861.
      Schnaper, H.W., et al. 1993. J. Cell. Physiol. 156, 235.
      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.
      Application referencesOriginal Clone Hurskainen, T., et al. 1996. J. Histochem. Cytochem. 44, 1379. Soini, Y., et al. 1994. J. Histochem. Cytochem. 42, 945.