| Code | CSB-RA110554A0HU |
| Size | US$210 |
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| Application | Recommended Dilution |
|---|---|
| WB | 1:500-1:5000 |
| IHC | 1:50-1:200 |
| FC | 1:50-1:200 |
Matrix metalloproteinase 11, also known as stromelysin-3, plays a distinctive role among the MMP family members in extracellular matrix remodeling and tissue homeostasis. Unlike most MMPs that are secreted as inactive zymogens, MMP11 undergoes intracellular activation, positioning it as a key player in processes involving stromal-epithelial interactions. Its expression patterns have made it particularly relevant to cardiovascular research and studies examining tissue remodeling dynamics.
This recombinant monoclonal antibody, generated from clone 7A10 in rabbit host, offers the reproducibility and consistency that demanding experimental workflows require. Because recombinant antibodies are produced from defined sequences rather than traditional hybridoma methods, you can expect reliable performance across experiments and between lot numbers, eliminating a common source of variability in long-term studies.
Validation testing demonstrates robust performance across multiple platforms. Western blot analysis confirms specific detection of MMP11 at the expected 55 kDa molecular weight across a diverse panel of human cell lines, including HepG2, COLO205, A549, K562, THP-1, HEK293, and SH-SY5Y lysates. This broad detection profile provides confidence when working with various cellular models. Immunohistochemistry validation in paraffin-embedded human prostate cancer tissue shows clear staining with standard citrate buffer antigen retrieval protocols. Flow cytometry analysis in HepG2 cells further demonstrates the antibody's utility for single-cell applications, showing distinct signal separation from isotype controls.
The antibody's compatibility with ELISA, western blotting, immunohistochemistry, and flow cytometry gives researchers flexibility to investigate MMP11 biology across complementary experimental approaches, supporting comprehensive characterization of this metalloproteinase in cardiovascular and tissue remodeling contexts.
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