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IM40 Anti-MMP-7 (Ab-1) Mouse mAb (141-7B2)

This Anti-MMP-7 (Ab-1) Mouse mAb (141-7B2) is validated for use in Immunoblotting, Paraffin Sections for the detection of MMP-7 (Ab-1).

Anti-MMP-7 (Ab-1) Mouse mAb (141-7B2) MSDS (material safety data sheet) or SDS, CoA and CoQ, dossiers, brochures and other available documents.

同义词: Anti-Matrilysin, Anti-Matrix Metalloproteinase 7, Anti-PUMP-1

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IM40
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概述

Replacement Information

重要规格表

Species ReactivityHostAntibody Type
HMMonoclonal Antibody

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      		 塑胶安瓿;塑胶针药瓶 100 μg
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      Description
      OverviewRecognizes the ~28 kDa latent form of MMP-7 in TPA-treated SW620 cells. Does not recognize the active form of MMP-7.
      Catalogue NumberIM40
      Brand Family Calbiochem®
      SynonymsAnti-Matrilysin, Anti-Matrix Metalloproteinase 7, Anti-PUMP-1
      Application Data
      Detection of MMP-7 by immunoblotting. Sample: E. coli.. Primary antibody: Anti-MMP-7 (Ab-1) Mouse mAb (141-7B2) (Cat. No. IM40) (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. 1991. FASEB J. 5, 2145.
      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., 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
      Quality LevelMQ100
      Applications
      Key Applications Immunoblotting (Western Blotting)
      Paraffin Sections
      Application NotesImmunoblotting (5-10 µg/ml, see application references)
      Paraffin Sections (see application references)
      Application CommentsDoes not recognize the ~19 kDa active form of MMP-7. To detect active MMP-7, use Cat. No. IM47L. Does not cross-react with human 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
      Immunogenhuman rectal carcinoma MMP-7
      ImmunogenHuman
      Clone141-7B2
      HostMouse
      IsotypeIgG₁
      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 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
      产品目录编号 GTIN
      IM40-100UGCN 04055977220599

      Documentation

      Anti-MMP-7 (Ab-1) Mouse mAb (141-7B2) MSDS

      职位

      物料安全数据表 (MSDS) 

      Anti-MMP-7 (Ab-1) Mouse mAb (141-7B2) 分析证书

      标题批号
      IM40

      参考

      参考信息概述
      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. 1991. FASEB J. 5, 2145.
      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., 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.
      数据表

      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 (5-10 µg/ml, see application references)
      Paraffin Sections (see application references)
      Application Data
      Detection of MMP-7 by immunoblotting. Sample: E. coli.. Primary antibody: Anti-MMP-7 (Ab-1) Mouse mAb (141-7B2) (Cat. No. IM40) (10 µg/ml). Detection: chemiluminescence.
      DescriptionPurified mouse monoclonal antibody. Recognizes the ~28 kDa latent 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 ~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 itself 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 in ~50% of gliomas.
      HostMouse
      Immunogen speciesHuman
      Immunogenhuman rectal carcinoma MMP-7
      Clone141-7B2
      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 ~19 kDa active form of MMP-7. To detect active MMP-7, use Cat. No. IM47L. Does not cross-react with human 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. 1991. FASEB J. 5, 2145.
      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., 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.