| Application | Recommended Dilution |
|---|---|
| IHC | 1:50-1:200 |
Matrix metalloproteinase-3, also known as stromelysin-1, plays a central role in extracellular matrix remodeling through its ability to degrade multiple ECM components including proteoglycans, fibronectin, laminin, and various collagen types. Beyond direct matrix degradation, MMP3 activates other MMPs in the proteolytic cascade, positioning it as a key regulatory node in tissue remodeling processes. This makes MMP3 a compelling target for cardiovascular research, where matrix turnover influences vascular integrity, atherosclerotic plaque stability, and cardiac tissue remodeling following injury.
This recombinant monoclonal antibody, clone 3B10, offers the reproducibility advantages that come with sequence-defined production. Unlike traditional hybridoma-derived antibodies, recombinant technology ensures consistent performance across lots, allowing you to establish protocols with confidence that your results will remain comparable over time and across experiments. The rabbit host and IgG isotype provide strong signal amplification potential, while affinity chromatography purification delivers a clean preparation suitable for demanding applications.
Validation in immunohistochemistry demonstrates reliable detection in human placenta tissue, where MMP3 expression reflects the extensive matrix remodeling characteristic of this tissue type. Testing on a Leica Bond automated system with citrate buffer antigen retrieval at pH 6.0 and overnight primary incubation at 4°C produced clear specific staining at 1:100 dilution, with the recommended working range of 1:50 to 1:200 offering flexibility to optimize signal intensity for your specific tissue context. The antibody is also validated for ELISA applications.
For researchers investigating cardiovascular pathology, tissue remodeling, or MMP biology more broadly, this antibody provides a dependable tool for localizing MMP3 expression in human tissue specimens.
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