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IM56 Anti-TIMP-2 (Ab-2) Mouse mAb (67-4H11)

IM56
  
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      Overview

      Replacement Information

      Key Spec Table

      Host
      M
      Description
      Overview

      This product has been discontinued.





      Recognizes the ~21-28 kDa TIMP-2 protein.
      Catalogue NumberIM56
      Brand Family Calbiochem®
      SynonymsAnti-Tissue Inhibitor of Metalloproteinase-2
      Application Data
      Detection of hamster TIMP-2 by immunoblotting. Sample: Expressed in CHO cells. Primary antibody: Anti-TIMP-2 (Ab-2) Mouse mAb (67-4H11) (Cat. No. IM56) (1 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 Sem. Cancer Biol., 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 controlTIMP-1 protein (Cat. No. PF019)
      Positive controlhTIMP-2 protein (Cat. No. PF021)
      Preservative≤0.1% sodium azide
      Applications
      Key Applications Frozen Sections
      Immunoblotting (Western Blotting)
      Paraffin Sections
      Application NotesFrozen Sections (1 µg/ml)
      Immunoblotting (5 µg/ml)
      Paraffin Sections (5 µg/ml, see application references)
      Application CommentsTIMP-2 is found in most cells and tissues in low amounts. Antibody should be titrated for optimal results in individual systems.
      Biological Information
      Immunogena synthetic peptide (YRGAAPPKQEFLDIED) corresponding to amino acids 178-193 in the C-terminal region of human TIMP-2
      ImmunogenHuman
      Clone67-4H11
      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

      Documentation

      Anti-TIMP-2 (Ab-2) Mouse mAb (67-4H11) Certificates of Analysis

      TitleLot Number
      IM56

      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 Sem. Cancer Biol., ed. M. M. Gottesman. Vol. 1(2), 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.

      Revision05-September-2007 JSW
      SynonymsAnti-Tissue Inhibitor of Metalloproteinase-2
      ApplicationFrozen Sections (1 µg/ml)
      Immunoblotting (5 µg/ml)
      Paraffin Sections (5 µg/ml, see application references)
      Application Data
      Detection of hamster TIMP-2 by immunoblotting. Sample: Expressed in CHO cells. Primary antibody: Anti-TIMP-2 (Ab-2) Mouse mAb (67-4H11) (Cat. No. IM56) (1 µg/ml). Detection: chemiluminescence.
      DescriptionPurified mouse monoclonal antibody (see application references). 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 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 (also called CSC-21K) is a 21 kDa unglycosylated protein that is expressed by a variety of cell types. It forms a non-covalent, stoichiometric complex with both latent and active MMPs, showing a preference for MMP-2.
      HostMouse
      Immunogen speciesHuman
      Immunogena synthetic peptide (YRGAAPPKQEFLDIED) corresponding to amino acids 178-193 in the C-terminal region of human TIMP-2
      Clone67-4H11
      IsotypeIgG₁
      Speciesbovine, guinea pig, human, mouse, rabbit, rat
      Positive controlhTIMP-2 protein (Cat. No. PF021)
      Negative controlTIMP-1 protein (Cat. No. PF019)
      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
      CommentsTIMP-2 is found in most cells and tissues in low amounts. 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.
      Woessner, J. F., 1991. FASEB J. 5, 2145.
      Liotta, L. A. and Stetler-Stevenson, W. G., 1990. in Sem. Cancer Biol., ed. M. M. Gottesman. Vol. 1(2), 99.