IM71 Anti-MMP-7 (Ab-3) Mouse mAb (ID2)

IM71
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Overview

Replacement Information

Key Specifications Table

Species ReactivityHostAntibody Type
H M Monoclonal Antibody

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IM71-100UG
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      Plastic ampoule 100 μg
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      Description
      OverviewRecognizes the ~28 kDa latent and the ~19 kDa active forms of MMP-7 in SW620 cells and bladder, breast, and ovarian carcinoma tissue.
      Catalogue NumberIM71
      Brand Family Calbiochem®
      SynonymsAnti-PUMP-1, Anti-Matrilysin, Anti-Matrix Metalloproteinase 7
      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.
      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.
      McDonnell, S., et al. 1994. Biochem. Soc. Trans. 22, 58.
      Cottam, D.W. and Rees, R.C. 1993. Intl. J. Oncol. 2, 861.
      Stetler-Stevenson, W.G. 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.
      Sellers, A. and Woessner, J.F., Jr. 1980. Biochem. J. 189, 521.
      Product Information
      DeclarationNot available for sale in Japan.
      FormLiquid
      FormulationIn 10 mM PBS, pH 7.4.
      Positive controlConditioned, serum-free medium from SW620 cells or bladder, breast, or ovarian carcinoma
      PreservativeNone
      Quality LevelMQ100
      Applications
      Application ReferencesImmunoblotting Windsor, L.J., et al. 1997. J. Biochim. Biophys. Acta 1334, 261.
      Key Applications Paraffin Sections
      Affinity Purification
      Immunoblotting (Western Blotting)
      Immunofluorescence
      Application NotesAffinity Purification (see comments)
      Immunoblotting (see application references)
      Immunofluorescence (see comments)
      Paraffin Sections (4-8 µg/ml, no pre-treatment required)
      Application CommentsThis antibody has also been reported to work for immunofluorescence and affinity purification methods. Antibody should be titrated for optimal results in individual systems.
      Biological Information
      Immunogenrecombinant human MMP-7
      ImmunogenHuman
      CloneID2
      HostMouse
      IsotypeIgG2b
      Species Reactivity
      • Human
      Antibody TypeMonoclonal Antibody
      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

      Documentation

      Anti-MMP-7 (Ab-3) Mouse mAb (ID2) Certificates of Analysis

      TitleLot Number
      IM71

      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.
      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.
      McDonnell, S., et al. 1994. Biochem. Soc. Trans. 22, 58.
      Cottam, D.W. and Rees, R.C. 1993. Intl. J. Oncol. 2, 861.
      Stetler-Stevenson, W.G. 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.
      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.

      Revision02-March-2009 JSW
      SynonymsAnti-PUMP-1, Anti-Matrilysin, Anti-Matrix Metalloproteinase 7
      ApplicationAffinity Purification (see comments)
      Immunoblotting (see application references)
      Immunofluorescence (see comments)
      Paraffin Sections (4-8 µg/ml, no pre-treatment required)
      DescriptionPurified mouse monoclonal antibody generated by immunizing BALB/c mice with the specified immunogen and fusing splenocytes with p3-X63-Ag8.653 mouse myeloma cells. Recognizes both the ~28 kDa latent and the ~18 kDa active forms of MMP-7.
      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. Matrix metalloproteinase-7 (MMP-7) also known as matrilysin and PUMP (EC 3.4.24.23) cleaves a number of substrates including collagen types IV and X, elastin, fibronectin, gelatin, laminin and proteoglycans. MMP-7 is closely related to the stromelysin family members but is encoded by a different gene. MMP-7 is the smallest of all the MMPs consisting of a pro-peptide domain and a catalytic domain. It lacks the hemopexin-like domain common to other members of the MMPs. MMP-7 is secreted as a 28 kDa proenzyme and can be activated in vitro by organomercurials (e.g., 4-aminophenylmercuric acetate, APMA) and trypsin and in vivo by MMP-3 to a 18 kDa active MMP-7 enzyme. Once activated, MMP-7 can activate pro-MMP-1 and pro-MMP-9 but not pro-MMP-2. MMP-7 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 ~50% of gliomas.
      HostMouse
      Immunogen speciesHuman
      Immunogenrecombinant human MMP-7
      CloneID2
      IsotypeIgG2b
      Specieshuman
      Positive controlConditioned, serum-free medium from SW620 cells or bladder, breast, or ovarian carcinoma
      FormLiquid
      FormulationIn 10 mM PBS, pH 7.4.
      Concentration Label Please refer to vial label for lot-specific concentration
      PreservativeNone
      CommentsThis antibody has also been reported to work for immunofluorescence and affinity purification methods. Antibody should be titrated for optimal results in individual systems.
      Storage -20°C
      Avoid freeze/thaw
      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.
      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.
      McDonnell, S., et al. 1994. Biochem. Soc. Trans. 22, 58.
      Cottam, D.W. and Rees, R.C. 1993. Intl. J. Oncol. 2, 861.
      Stetler-Stevenson, W.G. 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.
      Sellers, A. and Woessner, J.F., Jr. 1980. Biochem. J. 189, 521.
      Application referencesImmunoblotting Windsor, L.J., et al. 1997. J. Biochim. Biophys. Acta 1334, 261.