Millipore Sigma Vibrant Logo

IM38 Anti-MMP-8 (Ab-1) Mouse mAb (115-13D2)

Anti-MMP-8 (Ab-1) Mouse mAb (115-13D2): Ficha de datos de seguridad (MSDS o SDS), certificado de análisis y de calidad (CoA y CoQ), expedientes, folletos y otros documentos disponibles.

Sinónimos: Anti-Matrix Metalloproteinase 8, Anti-Neutrophil Collagenase

IM38
  
Recuperando precio...
No pudo obtenerse el precio
La cantidad mínima tiene que ser múltiplo de
Maximum Quantity is
Al finalizar el pedido Más información
Ahorró ()
 
—
Solicitar precio
—
Disponibilidad a confirmar Disponibilidad a confirmar
Ingrese cantidad 
Suspendido
Cantidades limitadas disponibles
Debe confirmarse disponibilidad
    El resto: se avisará
      El resto: se avisará
      Se avisará
      Póngase en contacto con el Servicio de Atención al Cliente
      Contact Customer Service

       

      Póngase en contacto con el Servicio de Atención al Cliente

      Descripción

      Replacement Information

      Tabla espec. clave

      Host
      M
      Description
      Overview

      This product has been discontinued.





      Recognizes the ~85 kDa latent and ~64 kDa active forms of MMP-8.
      Catalogue NumberIM38
      Brand Family Calbiochem®
      SynonymsAnti-Matrix Metalloproteinase 8, Anti-Neutrophil Collagenase
      Application Data
      Detection of human MMP-8 by immunoblotting. Sample: Tissue extract from human placenta. Primary antibody: Anti-MMP-8 (Ab-1) Mouse mAb (115-13D2) (Cat. No. IM38) (5 µg/ml). Detection: chemiluminescence.
      References
      ReferencesTakino, T., et al. 1995. J. Biol. Chem. 270, 23013.
      Cottam, D. W. and Rees, R. C. 1993. Intl J. Oncol. 2, 861.
      Knauper, V., et al. 1993. Biochem. J. 291, 847.
      Stetler-Stevenson, W. G., et al. 1993. FASEB J. 7, 1434.
      Blaser, J., et al. 1991. Eur. J. Biochem. 202, 1223.
      Woessner, J. F., 1991. FASEB J. 5, 2145.
      Knauper, V., et al. 1990. Eur. J. Biochem. 189, 295.
      Liotta, L. A. and Stetler-Stevenson, W. G., 1990. in Sem. Cancer Biol., ed. M. M. Gottesman. Vol. 1, 99.
      Lazarus, G.S., et al. 1968. J. Clin. Invest. 47, 2622.
      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.
      Preservative≤0.1% sodium azide
      Applications
      Application ReferencesParaffin Sections Matsuki, H., et al. 1996. Clin. Chim Acta 244, 129.
      Key Applications Immunoblotting (Western Blotting)
      Paraffin Sections
      Application NotesImmunoblotting (5 µg/ml)
      Paraffin Sections (see application references)
      Application CommentsThis antibody does not cross-react with human MMP-1, MMP-2, MMP-3, MMP-7, MMP-9, or MMP-13. For paraffin sections, fix with PLP (perioddate-lysine-4% paraformaldehyde) and culture tissue in monensin prior to fixation (see application reference). Antibody should be titrated for optimal results in individual systems.
      Biological Information
      Immunogenhuman MMP-8
      ImmunogenHuman
      Clone115-13D2
      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
      Número de referencia GTIN
      IM38 0

      Documentation

      Anti-MMP-8 (Ab-1) Mouse mAb (115-13D2) Certificados de análisis

      CargoNúmero de lote
      IM38

      Referencias bibliográficas

      Visión general referencias
      Takino, T., et al. 1995. J. Biol. Chem. 270, 23013.
      Cottam, D. W. and Rees, R. C. 1993. Intl J. Oncol. 2, 861.
      Knauper, V., et al. 1993. Biochem. J. 291, 847.
      Stetler-Stevenson, W. G., et al. 1993. FASEB J. 7, 1434.
      Blaser, J., et al. 1991. Eur. J. Biochem. 202, 1223.
      Woessner, J. F., 1991. FASEB J. 5, 2145.
      Knauper, V., et al. 1990. Eur. J. Biochem. 189, 295.
      Liotta, L. A. and Stetler-Stevenson, W. G., 1990. in Sem. Cancer Biol., ed. M. M. Gottesman. Vol. 1, 99.
      Lazarus, G.S., et al. 1968. J. Clin. Invest. 47, 2622.
      Ficha técnica

      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-July-2007 JSW
      SynonymsAnti-Matrix Metalloproteinase 8, Anti-Neutrophil Collagenase
      ApplicationImmunoblotting (5 µg/ml)
      Paraffin Sections (see application references)
      Application Data
      Detection of human MMP-8 by immunoblotting. Sample: Tissue extract from human placenta. Primary antibody: Anti-MMP-8 (Ab-1) Mouse mAb (115-13D2) (Cat. No. IM38) (5 µg/ml). Detection: chemiluminescence.
      DescriptionPurified mouse monoclonal antibody. Recognizes the ~85 kDa latent and the ~64 kDa active forms of MMP-8.
      BackgroundMatrix metalloproteinases (MMP's) are a family of enzymes that are responsible for the degradation of extracellular matrix components. Of the eleven proteins reported to date, ten are normally found as soluble molecules. MMP-8, also known as polymorphonuclear leukocyte collagenase, is a collagenolytic enzyme first described in 1986. MMP-8 is closely related to the fibroblast collagenases (47% homology) but is encoded by a different gene. The enzyme exists as an inactive pro form with a molecular weight of approximately 85 kDa of which 35% is contributed by glycosylation. MMP-8 becomes activated by removal of the amino terminal pro-peptide which can be effected by trypsin but not by cell bound plasmin in a two step process. MMP-8 also will undergo autoproteolysis a process which can also be mediated by mercurial compounds. Both processes are inhibited by TIMP-1 and TIMP-2, which bind to the catalytic domain of the enzyme with a 1:1 stoichiometry and is partially resistant to dissociation under SDS-PAGE conditions. The active enzyme has been found to be unstable at 37°C, breaking down into two fragments of 40 kDa and about 27 kDa. Of the two fragments the 40 kDa one has been identified as the catalytic domain and is biologically active while the other is the COOH terminal domain and is inactive.
      HostMouse
      Immunogen speciesHuman
      Immunogenhuman MMP-8
      Clone115-13D2
      IsotypeIgG₁
      Specieshuman
      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
      CommentsThis antibody does not cross-react with human MMP-1, MMP-2, MMP-3, MMP-7, MMP-9, or MMP-13. For paraffin sections, fix with PLP (perioddate-lysine-4% paraformaldehyde) and culture tissue in monensin prior to fixation (see application reference). 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
      ReferencesTakino, T., et al. 1995. J. Biol. Chem. 270, 23013.
      Cottam, D. W. and Rees, R. C. 1993. Intl J. Oncol. 2, 861.
      Knauper, V., et al. 1993. Biochem. J. 291, 847.
      Stetler-Stevenson, W. G., et al. 1993. FASEB J. 7, 1434.
      Blaser, J., et al. 1991. Eur. J. Biochem. 202, 1223.
      Woessner, J. F., 1991. FASEB J. 5, 2145.
      Knauper, V., et al. 1990. Eur. J. Biochem. 189, 295.
      Liotta, L. A. and Stetler-Stevenson, W. G., 1990. in Sem. Cancer Biol., ed. M. M. Gottesman. Vol. 1, 99.
      Lazarus, G.S., et al. 1968. J. Clin. Invest. 47, 2622.
      Application referencesParaffin Sections Matsuki, H., et al. 1996. Clin. Chim Acta 244, 129.