• Product name

    Anti-MMP26 antibody [EP1283Y]
  • Description

    Rabbit monoclonal [EP1283Y] to MMP26
  • Host species

  • 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 within Human MMP26 aa 200-300 (C terminal). The exact sequence is proprietary.

  • 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.

    We are constantly working hard to ensure we provide our customers with best in class antibodies. As a result of this work we are pleased to now offer this antibody in purified format. We are in the process of updating our datasheets. The purified format is designated 'PUR' on our product labels. If you have any questions regarding this update, please contact our Scientific Support team.



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

    • Database links

    • Alternative names

      • Endometase antibody
      • Matrilysin 2 antibody
      • Matrix Metalloproteinase 26 antibody
      • MMP 26 antibody


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

      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?


    This product has been referenced in:

    • Guo JG  et al. High MMP-26 expression in glioma is correlated with poor clinical outcome of patients. Oncol Lett 16:2237-2242 (2018). Read more (PubMed: 30008924) »
    See 1 Publication for this product

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