Overview

  • Product name
    Anti-MMP26 antibody [EP1283Y]
  • Description
    Rabbit monoclonal [EP1283Y] to MMP26
  • Tested applications
    Suitable for: WBmore details
    Unsuitable for: Flow Cyt,ICC,IHC-P or IP
  • Species reactivity
    Reacts with: Mouse, Rat, Human
  • Immunogen

    Synthetic peptide corresponding to residues near the C-terminus of human MMP26

  • Positive control
    • 293 cell lysate.
  • General notes

    Our RabMAb® technology is a patented hybridoma-based technology for making rabbit monoclonal antibodies. For details on our patents, please refer to RabMab® patents

Properties

Applications

Our Abpromise guarantee covers the use of ab81285 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

Application Abreviews Notes
WB 1/500 - 1/1000. Predicted molecular weight: 30 kDa.
  • Application notes
    Is unsuitable for Flow Cyt,ICC,IHC-P or IP.
  • Target

    • Relevance
      Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. MMP26, also known as Matrilysin 2, was first cloned from human fetal cells, and identified as an MMP most closely related to MMP7 (Matrilysin 1). The homology between MMP7 and MMP26 is low (only 38% identical), thus the functions are unlikely to be similar. Homology is much higher (48% identical) for the comparable region of MMP12, but MMP26 appears to have broader substrate specificity than does MMP12. MMP26, like MMP7, lacks the hemopexin domain common to the other MMPs, but contains a Propeptide domain, cysteine switch activation site, followed by a catalytic domain, and a short vestige of the hinge region. MMP26 is apparently not glycosylated, and is a secreted MMP. Tissue analysis shows MMP26 most strongly in placenta and uterus, but also in kidney cells, lung cells, lymphocytes and lung or endometrial carcinoma cells. MMP26 is proteolytically active, cleaving casein in zymograms, and gelatin, a1PI, fibrinogen, fibronectin, vitronectin, type IV collagen, and apparently activating MMP9. The proteolytic activity was blocked by TIMP1 and TIMP2. MMP26 does not appear to be produced by most normal quiescent cells, but treatment of many cell types with the phorbol ester TPA, or IL1 stimulates production of MMP26.
    • Cellular localization
      Secreted
    • Database links
    • Alternative names
      • Endometase antibody
      • Matrilysin 2 antibody
      • Matrix Metalloproteinase 26 antibody
      • MMP 26 antibody

    Images

    • Anti-MMP26 antibody [EP1283Y] (ab81285) at 1/500 dilution + 293 cell lysate at 10 µg

      Secondary
      HRP conjugated goat anti-rabbit at 1/2000 dilution

      Predicted band size : 30 kDa
      Observed band size : 18 kDa (why is the actual band size different from the predicted?)

    References

    ab81285 has not yet been referenced specifically in any publications.

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    Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"

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