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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) o SDS, certificato d’analisi (CoA) e certificato di qualità (CoQ), dossier, brochure e altri documenti disponibili.

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

IM40
Purchase on Sigma-Aldrich

Panoramica

Replacement Information

Tabella delle specifiche principali

Species ReactivityHostAntibody Type
HMMonoclonal Antibody

Products

Numero di catalogoConfezionamento Qtà/conf
IM40-100UG Fiala di plastica 100 μg
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
Numero di catalogo GTIN
IM40-100UG 04055977220599

Documentation

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

Titolo

Scheda di sicurezza (MSDS) 

Anti-MMP-7 (Ab-1) Mouse mAb (141-7B2) Certificati d'Analisi

TitoloNumero di lotto
IM40

Riferimenti bibliografici

Panoramica delle referenze
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.
Scheda tecnica

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.