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IM82 Anti-TIMP-2 (Ab-4) Mouse mAb (T2-N IC3)

IM82
  
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      Overview

      Replacement Information

      Key Specifications Table

      Host
      M
      Description
      Overview

      This product has been discontinued.





      Recognizes the ~21-28 kDa TIMP-2 protein conditioned medium from dexamethasone-treated HT1080 cells, melanoma, A2058 cells, and bladder, breast, and ovarian carcinoma.
      Catalogue NumberIM82
      Brand Family Calbiochem®
      SynonymsAnti-Tissue Inhibitor of Metalloproteinase-2
      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, 99.
      Product Information
      DeclarationNot available for sale in Japan.
      FormLiquid
      FormulationIn 10 mM PBS, 0.2% BSA, pH 7.4.
      Positive controlConditioned medium from dexamethasone-treated HT-1080 cells, melanoma A2058 cells, or bladder, breast, or ovarian carcinomas
      Preservative≤0.1% sodium azide
      Applications
      Key Applications Affinity Purification
      Frozen Sections
      Immunoblotting (Western Blotting)
      Paraffin Sections
      Application NotesAffinity Purification (see comments)
      Frozen Sections (1:50-1:100)
      Immunoblotting (1:200-1:400, chemiluminescence)
      Paraffin Sections (1:50-1:100, heat/pressure cooker pre-treatment required)
      Application CommentsThis antibody has been reported to work for affinity purification methods. Antibody should be titrated for optimal results in individual systems.
      Biological Information
      Immunogennative, human TIMP-2
      ImmunogenHuman
      CloneT2-N IC3
      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 +2°C to +8°C
      Do not freeze Ok to freeze
      Special InstructionsFor long-term storage, aliquot and freeze (-20°C). Avoid freeze/thaw cycles.
      Packaging Information
      Transport Information
      Supplemental Information
      Specifications
      Global Trade Item Number
      Catalog Number GTIN
      IM82 0

      Documentation

      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.
      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.

      Revision04-September-2007 RFH
      SynonymsAnti-Tissue Inhibitor of Metalloproteinase-2
      ApplicationAffinity Purification (see comments)
      Frozen Sections (1:50-1:100)
      Immunoblotting (1:200-1:400, chemiluminescence)
      Paraffin Sections (1:50-1:100, heat/pressure cooker pre-treatment required)
      DescriptionPurified mouse monoclonal antibody derived by immunizing BALB/c mice with the specified immunogen and fusing splenocytes with p3-X63-Ag8.653 mouse myeloma cells. Recognizes the ~21-28 kDa TIMP-2 protein.
      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 ~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 angiogenesis, arthritis, periodontitis, and metastasis. A family of endogenous inhibitors, tissue inhibitors of metalloproteinase (TIMP), regulate the activation and activity of MMPs. TIMPs are capable of altering the metastatic potential of cancer cells and have been shown to inhibit invasion and metastasis in animal models. TIMP-2 is a 194 amino acid unglycosylated protein of 21 kDa with 43% and 44% sequence homology to TIMP-1 and TIMP-3, respectively. TIMP-2 inhibits the activity of all active MMPs and regulates the activation of pro-MMP-2 by binding to the C-terminal region of pro-MMP-2 (Kd ~5 nM). As with TIMP-1, TIMP-2 has been shown to have erythroid potentiating activity and cell growth-promoting activity.
      HostMouse
      Immunogen speciesHuman
      Immunogennative, human TIMP-2
      CloneT2-N IC3
      IsotypeIgG₁
      Specieshuman
      Positive controlConditioned medium from dexamethasone-treated HT-1080 cells, melanoma A2058 cells, or bladder, breast, or ovarian carcinomas
      FormLiquid
      FormulationIn 10 mM PBS, 0.2% BSA, pH 7.4.
      Concentration Label Please refer to vial label for lot-specific concentration
      Preservative≤0.1% sodium azide
      CommentsThis antibody has been reported to work for affinity purification methods. Antibody should be titrated for optimal results in individual systems.
      Storage +2°C to +8°C
      Do Not Freeze Ok to freeze
      Special InstructionsFor long-term storage, aliquot and freeze (-20°C). Avoid freeze/thaw cycles.
      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, 99.