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IM33 Anti-MMP-2 (Ab-3) Mouse mAb (42-5D11)

This Anti-MMP-2 (Ab-3) Mouse mAb (42-5D11) is validated for use in Frozen Sections, Immunoblotting, Paraffin Sections for the detection of MMP-2 (Ab-3).

Anti-MMP-2 (Ab-3) Mouse mAb (42-5D11) MSDS (material safety data sheet) or SDS, CoA and CoQ, dossiers, brochures and other available documents.

Synonyms: Anti-72 kDa Gelatinase, Anti-Gelatinase A, Anti-Matrix Metalloproteinase 2

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IM33
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Overview

Replacement Information

Key Spec Table

Species ReactivityHostAntibody Type
B, H, M, RMMonoclonal Antibody

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IM33-100UG
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      		 Plastic ampoule 100 μg
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      Description
      OverviewRecognizes the ~72 kDa latent and the ~66 kDa active forms of the MMP-2.
      Catalogue NumberIM33
      Brand Family Calbiochem®
      SynonymsAnti-72 kDa Gelatinase, Anti-Gelatinase A, Anti-Matrix Metalloproteinase 2
      Application Data
      Detection of human MMP-2 by immunoblotting. Sample: Conditioned medium of normal human skin fibroblasts NB1RGB cells. Primary antibody: Anti-MMP-2 (Ab-3) Mouse mAb (42-5D11) (Cat. No. IM33) (2 µg/ml). Detection: chemiluminescence.
      References
      ReferencesCottam, D. W. and Rees, R. C. 1993. Intl J. Oncol. 2, 861.
      Fujimoto, N., et al. 1993. Clinica Chimica Acta. 221, 91.
      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
      Negative controlMMP-9 protein (Cat. Nos. PF024 or PF038)
      Positive controlMMP-2 protein (Cat. Nos. PF023 or PF037)
      Preservative≤0.1% sodium azide
      Quality LevelMQ100
      Applications
      Application ReferencesFrozen Sections Nakagawa, T., et al. 1994. J. Neurosurg. 81, 69. Immunoblotting, Original Clone Fujimoto, N., et al. 1993. Clinica Chimica Acta. 221, 91. Paraffin Sections Tsuchiya, Y., et al. 1994. Int. J. Cancer 56, 46.
      Key Applications Frozen Sections
      Immunoblotting (Western Blotting)
      Paraffin Sections
      Application NotesFrozen Sections (see application references)
      Immunoblotting (1 µg/ml)
      Paraffin Sections (see application references)
      Application CommentsThis antibody will not cross-react with human MMP-1, MMP-3, MMP-9, or MMP-13. Antibody should be titrated for optimal results in individual systems.
      Biological Information
      Immunogena synthetic peptide (VTPRDKPMGPLLVATF) corresponding to amino acids 468-483 of human MMP-2
      ImmunogenHuman
      Epitopewithin amino acids 468-483 of human MMP-2 (numbered from the propeptide)
      Clone42-5D11
      HostMouse
      IsotypeIgG₁
      Species Reactivity
      • Bovine
      • Human
      • Mouse
      • Rat
      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
      Catalogue Number GTIN
      IM33-100UG 07790788053772

      Documentation

      Anti-MMP-2 (Ab-3) Mouse mAb (42-5D11) SDS

      Title

      Safety Data Sheet (SDS) 

      Anti-MMP-2 (Ab-3) Mouse mAb (42-5D11) Certificates of Analysis

      TitleLot Number
      IM33

      References

      Reference overview
      Cottam, D. W. and Rees, R. C. 1993. Intl J. Oncol. 2, 861.
      Fujimoto, N., et al. 1993. Clinica Chimica Acta. 221, 91.
      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.

      Brochure

      Title
      Angiogenesis and Tumor Metastasis Brochure and Technical Guide
      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.

      Revision20-July-2007 JSW
      SynonymsAnti-72 kDa Gelatinase, Anti-Gelatinase A, Anti-Matrix Metalloproteinase 2
      ApplicationFrozen Sections (see application references)
      Immunoblotting (1 µg/ml)
      Paraffin Sections (see application references)
      Application Data
      Detection of human MMP-2 by immunoblotting. Sample: Conditioned medium of normal human skin fibroblasts NB1RGB cells. Primary antibody: Anti-MMP-2 (Ab-3) Mouse mAb (42-5D11) (Cat. No. IM33) (2 µg/ml). Detection: chemiluminescence.
      DescriptionPurified mouse monoclonal antibody (see application references). Recognizes the ~72 kDa latent and the ~66 kDa active forms of MMP-2.
      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-2 (Gelatinase A, 72 kDa gelatinase/type IV collagenase, TBE-1) is secreted as a 72 kDa zymogen which is proteolytically processed to the 66 kDa active form. MMP-2, along with its most closely related member of the MMP family, MMP-9, show substrate specificity toward type IV and V collagens, gelatin, and elastin. Numerous studies have shown a correlation between collagenase expression and metastatic potential, and suggest that it may be a useful marker for the diagnosis or prognosis of cancer.
      HostMouse
      Immunogen speciesHuman
      Immunogena synthetic peptide (VTPRDKPMGPLLVATF) corresponding to amino acids 468-483 of human MMP-2
      Epitopewithin amino acids 468-483 of human MMP-2 (numbered from the propeptide)
      Clone42-5D11
      IsotypeIgG₁
      Speciesbovine, human, mouse, rat
      Positive controlMMP-2 protein (Cat. Nos. PF023 or PF037)
      Negative controlMMP-9 protein (Cat. Nos. PF024 or PF038)
      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 will not cross-react with human MMP-1, MMP-3, MMP-9, or MMP-13. 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.
      Fujimoto, N., et al. 1993. Clinica Chimica Acta. 221, 91.
      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.
      Application referencesFrozen Sections Nakagawa, T., et al. 1994. J. Neurosurg. 81, 69. Immunoblotting, Original Clone Fujimoto, N., et al. 1993. Clinica Chimica Acta. 221, 91. Paraffin Sections Tsuchiya, Y., et al. 1994. Int. J. Cancer 56, 46.