Related Experiment Video
Updated: Jul 16, 2026

In Vivo Immunofluorescence Localization for Assessment of Therapeutic and Diagnostic Antibody Biodistribution in Cancer Research
Published on: September 16, 2019
A rat monoclonal antibody that recognizes pro- and active MMP-7 indicates polarized expression in vivo
Barbara Fingleton1, William C Powell, Howard C Crawford
1Department of Cancer Biology, Vanderbilt University Medical Center, Nashville, Tennessee 37232-6840, USA. Barbara.Fingleton@Vanderbilt.edu
Abstract:
Matrix metalloproteinases (MMPs) are a family of enzymes named for their ability to degrade proteins of the extracellular matrix. Here we describe the characterization of a rat monoclonal antibody specifically recognizing one member of this enzyme family, MMP-7. This antibody has been tested for its use in multiple assay types and was shown to be useful for direct enzyme-linked immunosorbent assay (ELISA), Western blotting, immunocytochemistry, and immunohistochemistry of frozen or paraffin-embedded tissues. The antibody has been evaluated for its usefulness with tissues from several different species and, by immunohistochemistry, can detect MMP-7 of human, murine, porcine, and gerbil origin. Immunostaining of MMP-7 in normal tissues or benign tumors of intestinal, breast, and prostatic origin indicates that this protein is normally localized luminally in glandular epithelium. The localization pattern would suggest that in normal or early stage tumors, MMP-7 is most likely not directly involved in extracellular matrix degradation. In contrast, advanced colon tumors show MMP-7 in invading cells at the advancing edge of the tumor.
Insights
A new rat monoclonal antibody specifically recognizes matrix metalloproteinase-7 (MMP-7). This antibody is effective in various assays and detects MMP-7 across multiple species, aiding in understanding its role in cancer progression.
Area of Science:
- Biochemistry and Molecular Biology
- Immunology
- Oncology
Background:
- Matrix metalloproteinases (MMPs) are crucial enzymes involved in extracellular matrix degradation.
- MMP-7, a specific member of the MMP family, plays a role in various physiological and pathological processes.
- Understanding the precise localization and function of MMP-7 is vital for cancer research.
Purpose of the Study:
- To characterize a novel rat monoclonal antibody against human MMP-7.
- To evaluate the antibody's utility in diverse immunological and biochemical assays.
- To investigate the expression and localization of MMP-7 in normal and cancerous tissues across different species.
Main Methods:
- Development and characterization of a rat monoclonal antibody targeting MMP-7.
- Validation of the antibody using enzyme-linked immunosorbent assay (ELISA), Western blotting, immunocytochemistry, and immunohistochemistry.
- Testing antibody efficacy on frozen and paraffin-embedded tissues from multiple species (human, murine, porcine, gerbil).
- Immunohistochemical analysis of MMP-7 expression in normal tissues (intestinal, breast, prostate) and tumors.
Main Results:
- The developed rat monoclonal antibody specifically recognizes MMP-7.
- The antibody demonstrated high utility in ELISA, Western blotting, immunocytochemistry, and immunohistochemistry.
- MMP-7 was detected in human, murine, porcine, and gerbil tissues.
- In normal and benign tissues, MMP-7 showed luminal localization in glandular epithelium.
- Advanced colon tumors exhibited MMP-7 expression in invading cells at the tumor's leading edge.
Conclusions:
- A specific and versatile monoclonal antibody for MMP-7 has been successfully developed and characterized.
- This antibody is a valuable tool for detecting MMP-7 in various biological samples and species.
- MMP-7's localization suggests a role in extracellular matrix remodeling, particularly in advanced tumor invasion.
