Recombinant Mouse Stromelysin-1 (Mmp3) is produced in an E. coli expression system, spanning the full length of the mature protein from amino acids 104 to 477. The protein carries an N-terminal 6xHis tag, which aids in purification and detection. SDS-PAGE analysis confirms that purity levels exceed 90%. This product is designed for research use only and should not be used in diagnostic or therapeutic applications.
Stromelysin-1, also known as Mmp3, belongs to the matrix metalloproteinase (MMP) family. It appears to play a crucial role in breaking down extracellular matrix components, a process that seems vital for tissue remodeling and repair. Mmp3 participates in various physiological processes, including embryonic development, reproduction, and tissue resorption. Research suggests its activity may be particularly significant in studies of cancer, arthritis, and cardiovascular diseases, likely due to its involvement in matrix remodeling and cell signaling pathways.
Potential Applications
Note: The applications listed below are based on what we know about this protein's biological functions, published research, and experience from experts in the field. However, we haven't fully tested all of these applications ourselves yet. We'd recommend running some preliminary tests first to make sure they work for your specific research goals.
1. Matrix Metalloproteinase Enzyme Activity Studies
This recombinant mouse MMP3 can help investigate the proteolytic activity and substrate specificity of stromelysin-1 under controlled laboratory conditions. Researchers might use fluorogenic or chromogenic substrates to characterize the enzyme's kinetic parameters and optimal reaction conditions. The N-terminal His-tag makes purification and immobilization straightforward for enzyme assays, while the high purity (>90%) should provide reliable and reproducible results in biochemical studies.
2. Protein-Protein Interaction Analysis
The His-tagged recombinant MMP3 appears well-suited for pull-down assays and co-immunoprecipitation experiments aimed at identifying and characterizing protein binding partners. The tag allows efficient capture using nickel-based affinity chromatography systems, potentially helping researchers isolate MMP3-interacting proteins from cell lysates or tissue extracts. This approach may help reveal the molecular networks and regulatory mechanisms involving stromelysin-1 in various biological processes.
3. Antibody Development and Validation
This purified recombinant protein could serve as an immunogen for generating specific antibodies against mouse MMP3 or as a standard for validating existing antibodies. The high purity and defined sequence (aa 104-477) appear suitable for immunization protocols and subsequent antibody characterization studies. Researchers can apply this protein in ELISA, Western blot, and other immunoassays to assess antibody specificity and cross-reactivity.
4. Structural and Biophysical Characterization
The recombinant MMP3 protein might prove useful in structural biology studies including X-ray crystallography, NMR spectroscopy, or cryo-electron microscopy to understand the three-dimensional architecture of stromelysin-1. Biophysical techniques such as dynamic light scattering, circular dichroism spectroscopy, and thermal stability assays could provide insights into protein folding, stability, and conformational changes under different conditions.
5. Inhibitor Screening and Drug Discovery Research
This recombinant protein may serve as a valuable target for screening potential MMP3 inhibitors in drug discovery pipelines. Researchers could apply high-throughput screening assays to evaluate the inhibitory effects of small molecules, peptides, or natural compounds against the recombinant enzyme. The standardized protein preparation should enable consistent and comparable results across different screening campaigns and may help advance structure-activity relationship studies.
