IM37 Anti-MMP-9 (Ab-3) Mouse mAb (56-2A4)

This Anti-MMP-9 (Ab-3) Mouse mAb (56-2A4) is validated for use in Frozen Sections, Immunoblotting, Paraffin Sections for the detection of MMP-9 (Ab-3).

Anti-MMP-9 (Ab-3) Mouse mAb (56-2A4) MSDS (material safety data sheet) or SDS, CoA and CoQ, dossiers, brochures and other available documents.

Synonyms: Anti-Gelatinase B, Anti-92 kDa Gelatinase, Anti-Matrix Metalloproteinase 9

IM37
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      Overview

      Replacement Information

      Key Specifications Table

      Species ReactivityHostAntibody Type
      Gp, H, Rb, R M Monoclonal Antibody

      Pricing & Availability

      Catalog Number AvailabilityPackaging Qty/Pack Price Quantity
      IM37-100UG
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          		 Plastic ampoule 100 μg
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          Description
          OverviewRecognizes the ~92 kDa latent and the ~83 kDa active forms of MMP-9 in breast carcinoma tissue.
          Catalogue NumberIM37
          Brand Family Calbiochem®
          SynonymsAnti-Gelatinase B, Anti-92 kDa Gelatinase, Anti-Matrix Metalloproteinase 9
          Application Data
          Detection of human MMP-9 by immunoblotting. Sample: Conditioned medium of human fibrosarcoma HT1080 cells. Primary antibody: Anti-MMP-9 (Ab-3) Mouse mAb (56-2A4) (Cat. No. IM37) (2 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.
          Okada, Y., et al., 1992. J. Biol. Chem. 267, 21712.
          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, 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-2 protein (Cat. Nos. PF023 or PF037)
          Positive controlMMP-9 protein (Cat. Nos. PF024 or PF038) or breast carcinoma tissue
          Preservative≤0.1% sodium azide
          Applications
          Application ReferencesImmunoblotting, Original Clone Okada, Y., et al. 1992. J. Biol. Chem. 267, 21712. Immunohistochemistry Nakagawa, T., et al. 1994. J. Neurosurg. 81, 69. 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 does not react with MMP-1, MMP-2, MMP-3 or MMP-13. Antibody should be titrated for optimal results in individual systems.
          Biological Information
          Immunogena synthetic peptide corresponding to amino acids 626-644 of human MMP-9
          ImmunogenHuman
          Clone56-2A4
          HostMouse
          IsotypeIgG₁
          Species Reactivity
          • Guinea Pig
          • Human
          • Rabbit
          • 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 Dry 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

          Documentation

          Anti-MMP-9 (Ab-3) Mouse mAb (56-2A4) SDS

          Title

          Safety Data Sheet (SDS) 

          Anti-MMP-9 (Ab-3) Mouse mAb (56-2A4) Certificates of Analysis

          TitleLot Number
          IM37

          References

          Reference overview
          Cottam, D.W. and Rees, R.C. 1993. Intl. J. Oncol. 2, 861.
          Stetler-Stevenson, W.G., et al. 1993. FASEB J. 7, 1434.
          Okada, Y., et al., 1992. J. Biol. Chem. 267, 21712.
          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, 99.
          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.

          Revision22-February-2011 RFH
          SynonymsAnti-Gelatinase B, Anti-92 kDa Gelatinase, Anti-Matrix Metalloproteinase 9
          ApplicationFrozen Sections (see application references)
          Immunoblotting (1 µg/ml)
          Paraffin Sections (see application references)
          Application Data
          Detection of human MMP-9 by immunoblotting. Sample: Conditioned medium of human fibrosarcoma HT1080 cells. Primary antibody: Anti-MMP-9 (Ab-3) Mouse mAb (56-2A4) (Cat. No. IM37) (2 µg/ml). Detection: chemiluminescence.
          DescriptionPurified mouse monoclonal antibody (see application references). Recognizes both the ~92 kDa latent and the ~83 kDa active forms of MMP-9.
          BackgroundMatrix metalloproteinases (MMP's) 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 MMP's 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 ~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-9 (Gelatinase B, 92 kDa gelatinase/type IV collagenase) is secreted as a 92 kDa zymogen which is proteolytically processed to the 83 kDa active form. MMP-9 shows substrate specificity toward type IV and V collagens, gelatin and elastin.
          HostMouse
          Immunogen speciesHuman
          Immunogena synthetic peptide corresponding to amino acids 626-644 of human MMP-9
          Clone56-2A4
          IsotypeIgG₁
          Speciesnot bovine, guinea pig, not hamster, human, not mouse, rabbit, rat
          Positive controlMMP-9 protein (Cat. Nos. PF024 or PF038) or breast carcinoma tissue
          Negative controlMMP-2 protein (Cat. Nos. PF023 or PF037)
          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 react with MMP-1, MMP-2, MMP-3 or MMP-13. Antibody should be titrated for optimal results in individual systems.
          Storage -20°C
          Avoid freeze/thaw
          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.
          Okada, Y., et al., 1992. J. Biol. Chem. 267, 21712.
          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, 99.
          Application referencesImmunoblotting, Original Clone Okada, Y., et al. 1992. J. Biol. Chem. 267, 21712. Immunohistochemistry Nakagawa, T., et al. 1994. J. Neurosurg. 81, 69. Tsuchiya, Y., et al. 1994. Int. J. Cancer 56, 46.