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

This Anti-MMP-7 (Ab-3) Mouse mAb (ID2) is validated for use in Affinity Purification, Immunoblotting, Immunofluorescence, Paraffin Sections for the detection of MMP-7 (Ab-3).

Anti-MMP-7 (Ab-3) Mouse mAb (ID2) MSDS (material safety data sheet) or SDS, CoA and CoQ, dossiers, brochures and other available documents.

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

IM71
  
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Overview

Replacement Information

Key Spec Table

Species ReactivityHostAntibody Type
HMMonoclonal Antibody
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 Affinity Purification
Immunoblotting (Western Blotting)
Immunofluorescence
Paraffin Sections
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
Global Trade Item Number
Catalogue Number GTIN
IM71 0

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 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.
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.