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IM36 Anti-MMP-3 (Ab-1) Mouse mAb (55-2A4)

This Anti-MMP-3 (Ab-1) Mouse mAb (55-2A4) is validated for use in Frozen Sections, Immunoblotting, Paraffin Sections for the detection of MMP-3 (Ab-1).

Anti-MMP-3 (Ab-1) Mouse mAb (55-2A4) : FDS (Fiches de données de sécurité), certificats d’analyse (CoA) et de qualité (CoQ), dossiers, brochures et autres documents disponibles.
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IM36
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Aperçu

Replacement Information

Tableau de caractéristiques principal

Species ReactivityHostAntibody Type
H, Porcine, R, ShMMonoclonal Antibody

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IM36-100UG
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      Description
      OverviewRecognizes the ~57/59 kDa latent and the ~28/45 kDa active forms of MMP-3. Will also recognize MMP-3/TIMP-1 complexes. Slightly cross-reacts (~34%) with human MMP-10.
      Catalogue NumberIM36
      Brand Family Calbiochem®
      Application Data
      Detection of human MMP-3 by immunoblotting. Sample: Conditioned medium of normal human skin fibroblasts NB1RGB cells. Primary antibody: Anti-MMP-3 (Ab-1) Mouse mAb (55-2A4) (Cat. No. IM36) (0.5 µg/ml). Detection: chemiluminescence.
      References
      ReferencesCottam, 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 Seminars in Cancer Biology, ed. M.M. Gottesman. Vol. 1(2), 99.
      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
      Quality LevelMQ100
      Applications
      Key Applications Frozen Sections
      Immunoblotting (Western Blotting)
      Paraffin Sections
      Application NotesFrozen Sections (see application references)
      Immunoblotting (1 µg/ml)
      Paraffin Sections (see comments and application references)
      Application CommentsThis antibody has 34% cross-reactivity with human MMP-10. For paraffin sections, staining can be enhanced by culturing tissue in 2 µM monensin for 3 h. Pre-treating with trypsin or a pressure cooker may enhance staining. Tissue can then be fixed with PLP (perioddate-lysine-4% paraformaldehyde) and stained using 5-10 µg/ml MMP-3 antibody. See application references for more information. Clone 55-2A4 is called Clone B in Obata, K., et al. To prepare conditioned medium for positive control, incubate HT-1080 cells for 2 h at 37°C in serum-free media containing 100 nM PMA. Collect and centrifuge medium; concentrate as necessary. Store in aliquots at -20°C. Antibody should be titrated for optimal results in individual systems.
      Biological Information
      Immunogenhuman pro-MMP-3 from the conditioned media of rheumatoid synovial fibroblasts
      ImmunogenHuman
      Clone55-2A4
      HostMouse
      IsotypeIgG₁
      Species Reactivity
      • Human
      • Porcine
      • Rat
      • Sheep
      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
      Référence GTIN
      IM36-100UG 04055977220575

      Documentation

      Anti-MMP-3 (Ab-1) Mouse mAb (55-2A4) FDS

      Titre

      Fiche de données de sécurité des matériaux (FDS) 

      Anti-MMP-3 (Ab-1) Mouse mAb (55-2A4) Certificats d'analyse

      TitreNuméro de lot
      IM36

      Références bibliographiques

      Aperçu de la référence bibliographique
      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 Seminars in Cancer Biology, ed. M.M. Gottesman. Vol. 1(2), 99.
      Fiche technique

      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
      ApplicationFrozen Sections (see application references)
      Immunoblotting (1 µg/ml)
      Paraffin Sections (see comments and application references)
      Application Data
      Detection of human MMP-3 by immunoblotting. Sample: Conditioned medium of normal human skin fibroblasts NB1RGB cells. Primary antibody: Anti-MMP-3 (Ab-1) Mouse mAb (55-2A4) (Cat. No. IM36) (0.5 µg/ml). Detection: chemiluminescence.
      DescriptionPurified mouse monoclonal antibody (see application references). Recognizes the ~59/57 kDa latent and the ~45/28 kDa active forms of MMP-3 and MMP-3/TIMP complexes (see application references).
      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 approximately 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 arthritis, periodontitis, and metastasis. MMP-3 (stromelysin-1) is secreted as a 59/57 kDa zymogen that is proteolytically processed to the 45 and 28 kDa active forms. This enzyme degrades a wide spectrum of extracellular matrix proteins, including cartilage proteoglycans, fibronectin, type IV and IX collagen and laminin. MMP-3 is thought to play an important role in pathophysiological degradation processes associated with conditions such as rheumatoid arthritis and cancer cell invasion.
      HostMouse
      Immunogen speciesHuman
      Immunogenhuman pro-MMP-3 from the conditioned media of rheumatoid synovial fibroblasts
      Clone55-2A4
      IsotypeIgG₁
      Speciesnot bovine, human, not mouse, porcine, not rabbit, rat, sheep
      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 has 34% cross-reactivity with human MMP-10. For paraffin sections, staining can be enhanced by culturing tissue in 2 µM monensin for 3 h. Pre-treating with trypsin or a pressure cooker may enhance staining. Tissue can then be fixed with PLP (perioddate-lysine-4% paraformaldehyde) and stained using 5-10 µg/ml MMP-3 antibody. See application references for more information. Clone 55-2A4 is called Clone B in Obata, K., et al. To prepare conditioned medium for positive control, incubate HT-1080 cells for 2 h at 37°C in serum-free media containing 100 nM PMA. Collect and centrifuge medium; concentrate as necessary. Store in aliquots at -20°C. 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
      ReferencesCottam, 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 Seminars in Cancer Biology, ed. M.M. Gottesman. Vol. 1(2), 99.