Recombinant Human Urokinase-type plasminogen activator (PLAU) is expressed in E. coli and contains amino acids 21 to 173 of the protein. The protein carries an N-terminal 6xHis-tag, which makes purification and detection more straightforward. SDS-PAGE analysis shows a purity level that exceeds 90%, suggesting high quality for research applications. This product is designed for research use only and is not intended for clinical applications.
Urokinase-type plasminogen activator (uPA) is a serine protease that appears to be critical in converting plasminogen to plasmin, a key enzyme involved in fibrinolysis. It likely plays a significant role in extracellular matrix degradation and tissue remodeling, influencing processes such as cell migration and tissue repair. Scientists widely study uPA for its involvement in various physiological and pathological pathways, making it an important target in research.
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. In Vitro Protein-Protein Interaction Studies
This recombinant PLAU fragment (21-173aa) can be used to investigate protein-protein interactions involving the urokinase-type plasminogen activator in controlled laboratory settings. The N-terminal 6xHis tag allows for purification and immobilization in pull-down assays or surface plasmon resonance experiments. Scientists can examine binding partners, determine binding kinetics, and map interaction domains using this defined protein fragment. The high purity (>90%) may help ensure reliable and reproducible results in biochemical binding assays.
2. Antibody Development and Characterization
The recombinant PLAU protein serves as a useful immunogen or screening antigen for developing research antibodies against human urokinase-type plasminogen activator. The 6xHis tag makes protein purification and immobilization on various surfaces more manageable for ELISA-based antibody screening and characterization. Scientists can use this protein to validate antibody specificity, determine binding affinities, and establish standard curves for quantitative immunoassays. The defined amino acid sequence (21-173aa) allows for precise epitope mapping studies.
3. Structural and Biophysical Analysis
This partial PLAU protein fragment can be used for structural biology studies to understand the molecular architecture of specific domains within the urokinase-type plasminogen activator. The high purity and defined sequence make it suitable for techniques such as X-ray crystallography, NMR spectroscopy, or cryo-electron microscopy. Scientists can investigate conformational changes, domain organization, and structure-function relationships within this specific region of the protein. The 6xHis tag can be removed if needed for certain structural studies.
4. Biochemical Assay Development and Validation
The recombinant PLAU fragment can serve as a reference standard or positive control in developing biochemical assays targeting urokinase-type plasminogen activator. Scientists can use this protein to establish assay conditions, validate detection methods, and create standard curves for quantitative measurements. The consistent quality and defined composition appears to enable reproducible assay performance across different experimental conditions. The protein can also be used to test the specificity of newly developed detection reagents or analytical methods.
