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IM47 Anti-MMP-7 (Ab-2) Mouse mAb (176-5F12)

Anti-MMP-7 (Ab-2) Mouse mAb (176-5F12) MSDS (material safety data sheet) or SDS, CoA and CoQ, dossiers, brochures and other available documents.

Synonyms: Anti-Matrilysin, Anti-Matrix Metalloproteinase 7, Anti-PUMP-1

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      Overview

      Replacement Information

      Key Spec Table

      Host
      M
      Description
      Overview

      This product has been discontinued.





      Recognizes the ~19 kDa active form of MMP-7 in CaR-1 cells and TPA-treated SW620 cells. Does not recognize the latent form of MMP-7.
      Catalogue NumberIM47
      Brand Family Calbiochem®
      SynonymsAnti-Matrilysin, Anti-Matrix Metalloproteinase 7, Anti-PUMP-1
      Application Data
      Detection of human MMP-7 by immunoblotting. Sample: Conditioned medium of human rectal carcinoma CaR-1 cells. Primary antibody: Anti-MMP-7 (Ab-2) Mouse mAb (176-5F12) (Cat. No. IM47) (10 µg/ml). Detection: chemiluminescence.
      References
      ReferencesBrunner, K.L, et al. 1995. Proc. Natl. Acad. Sci. USA 92, 7362.
      Imai, K., et al. 1995. J. Biol. Chem. 270, 6691.
      Lichtinghagen, R., et al. 1995. Eur. J. Clin. Chem. Clin. Biochem. 33, 65.
      Nakano, A., et al. 1995. J. Neurosurg. 83, 298.
      Takino, T., et al. 1995. J. Biol. Chem. 270, 23013.
      Woessner, J.F., Jr., 1995. Meth. Enzymol. 248, 485.
      Yamamoto, H., et al. 1995. J. Clin. Lab. Anal. 9, 297.
      Gaire, M., et al. 1994. J. Biol. Chem. 269, 2032.
      Woessner, J.F., Jr., 1995. Meth. Enzymol. 248, 485.
      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 Sem. Cancer Biol., ed. M. M. Gottesman. Vol. 1(2), 99.
      Woessner, J.F., Jr and Taplin, C.J., 1988. J. Biol. Chem. 263, 16918.
      Sellers, A and Woessner, J.F., Jr., 1980. Biochem. J. 189, 521.
      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 controlCaR-1 or TPA-treated SW620 cells
      Preservative≤0.1% sodium azide
      Applications
      Key Applications Immunoblotting (Western Blotting)
      Application NotesImmunoblotting (10 µg/ml)
      Application CommentsDoes not recognize the latent form of MMP-7 (28 kDa). To detect latent MMP-7, use Cat. No. IM40L. Does not cross-react with MMP-1, MMP-2, MMP-3, MMP-8, MMP-9 or MMP-13. For optimal detection, SW620 cells should be treated with TPA (100 ng/ml) to induce expression of MMP-7. Antibody should be titrated for optimal results in individual systems.
      Biological Information
      Immunogena synthetic peptide (YSLFP) corresponding to amino acids 78-82 of human MMP-7
      ImmunogenHuman
      Clone176-5F12
      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 -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
      IM47 0

      Documentation

      Anti-MMP-7 (Ab-2) Mouse mAb (176-5F12) Certificates of Analysis

      TitleLot Number
      IM47

      References

      Reference overview
      Brunner, K.L, et al. 1995. Proc. Natl. Acad. Sci. USA 92, 7362.
      Imai, K., et al. 1995. J. Biol. Chem. 270, 6691.
      Lichtinghagen, R., et al. 1995. Eur. J. Clin. Chem. Clin. Biochem. 33, 65.
      Nakano, A., et al. 1995. J. Neurosurg. 83, 298.
      Takino, T., et al. 1995. J. Biol. Chem. 270, 23013.
      Woessner, J.F., Jr., 1995. Meth. Enzymol. 248, 485.
      Yamamoto, H., et al. 1995. J. Clin. Lab. Anal. 9, 297.
      Gaire, M., et al. 1994. J. Biol. Chem. 269, 2032.
      Woessner, J.F., Jr., 1995. Meth. Enzymol. 248, 485.
      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 Sem. Cancer Biol., ed. M. M. Gottesman. Vol. 1(2), 99.
      Woessner, J.F., Jr and Taplin, C.J., 1988. J. Biol. Chem. 263, 16918.
      Sellers, A and Woessner, J.F., Jr., 1980. Biochem. J. 189, 521.
      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.

      Revision27-August-2007 RFH
      SynonymsAnti-Matrilysin, Anti-Matrix Metalloproteinase 7, Anti-PUMP-1
      ApplicationImmunoblotting (10 µg/ml)
      Application Data
      Detection of human MMP-7 by immunoblotting. Sample: Conditioned medium of human rectal carcinoma CaR-1 cells. Primary antibody: Anti-MMP-7 (Ab-2) Mouse mAb (176-5F12) (Cat. No. IM47) (10 µg/ml). Detection: chemiluminescence.
      DescriptionPurified mouse monoclonal antibody. Recognizes the ~19 kDa active form of MMP-7.
      BackgroundThe matrix metalloproteinases (MMP's) are a family of enzymes responsible for the degradation of extracellular matrix components. Of the eleven proteins reported to date, ten are normally found as soluble molecules. MMP-7, also known as matrilysin, is responsible for hydrolyzing proteoglycans and extracellular matrix glycoproteins and was first described in 1980 but not purified to homogeneity until 1988. MMP-7 is closely related to the stromelysin family members but is encoded by a different gene. The enzyme exists as an inactive pro form with a molecular weight of approximately 28 kDa (range: 28-30 kDa) which becomes activated by proteolytic cleavage to an active 19 kDa form. Pro-MMP-7 may be activated by trypsin, mercurial compounds or by MMP-3 and once activated can activate pro-MMP-1 and pro-MMP-9 but not pro-MMP-2. MMP-7 is distinguished from the other MMP family members as being the smallest member containing only the common catalytic domain and the Zn2+ binding region but missing the hemopexin-like domain common to the other MMP's. Matrilysin is widely expressed having been reported in elevated levels in cycling endometrium as well as in colorectal cancers and adenomas, hepatocellular carcinomas, rectal carcinomas, and approximately 50% of gliomas.
      HostMouse
      Immunogen speciesHuman
      Immunogena synthetic peptide (YSLFP) corresponding to amino acids 78-82 of human MMP-7
      Clone176-5F12
      IsotypeIgG₁
      Specieshuman
      Positive controlCaR-1 or TPA-treated SW620 cells
      FormLiquid
      FormulationIn 100 mM sodium phosphate buffer, 0.1% BSA, pH 7.0.
      Concentration Label Please refer to vial label for lot-specific concentration
      Preservative≤0.1% sodium azide
      CommentsDoes not recognize the latent form of MMP-7 (28 kDa). To detect latent MMP-7, use Cat. No. IM40L. Does not cross-react with MMP-1, MMP-2, MMP-3, MMP-8, MMP-9 or MMP-13. For optimal detection, SW620 cells should be treated with TPA (100 ng/ml) to induce expression of MMP-7. 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
      ReferencesBrunner, K.L, et al. 1995. Proc. Natl. Acad. Sci. USA 92, 7362.
      Imai, K., et al. 1995. J. Biol. Chem. 270, 6691.
      Lichtinghagen, R., et al. 1995. Eur. J. Clin. Chem. Clin. Biochem. 33, 65.
      Nakano, A., et al. 1995. J. Neurosurg. 83, 298.
      Takino, T., et al. 1995. J. Biol. Chem. 270, 23013.
      Woessner, J.F., Jr., 1995. Meth. Enzymol. 248, 485.
      Yamamoto, H., et al. 1995. J. Clin. Lab. Anal. 9, 297.
      Gaire, M., et al. 1994. J. Biol. Chem. 269, 2032.
      Woessner, J.F., Jr., 1995. Meth. Enzymol. 248, 485.
      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 Sem. Cancer Biol., ed. M. M. Gottesman. Vol. 1(2), 99.
      Woessner, J.F., Jr and Taplin, C.J., 1988. J. Biol. Chem. 263, 16918.
      Sellers, A and Woessner, J.F., Jr., 1980. Biochem. J. 189, 521.