Recombinant Human Tissue-type plasminogen activator (PLAT) (R497Q) comes from a baculovirus expression system. This version represents the complete mature protein spanning amino acids 36 to 562, though it carries a specific R497Q mutation. Scientists have added both an N-terminal 10xHis-tag and a C-terminal Myc-tag to make detection and purification more straightforward. SDS-PAGE analysis shows the product maintains purity levels above 85%, which appears suitable for most research applications.
Tissue-type plasminogen activator (tPA) functions as a serine protease that breaks down blood clots. It does this by converting plasminogen into plasmin. This protein plays a crucial role in fibrinolysis—a process that seems essential for keeping our vascular system healthy. Given its significance in thrombolytic therapy, researchers frequently study tPA in cardiovascular and blood-related research. These studies may offer valuable insights into therapeutic approaches for clot-related disorders.
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. Protein-Protein Interaction Studies
This dual-tagged PLAT variant works well in pull-down assays for identifying and studying the binding partners of tissue-type plasminogen activator. The N-terminal His-tag lets researchers attach it to nickel-based resins. Meanwhile, the C-terminal Myc-tag helps with detection and confirms protein capture through anti-Myc antibodies. The R497Q mutation creates an interesting opportunity—scientists can examine how this particular amino acid change might alter protein interactions when compared to the normal PLAT version. Studies like these could shed light on the molecular mechanisms that drive PLAT function and regulation.
2. Structural and Biochemical Characterization
Researchers can use this recombinant protein for detailed structural analysis. This might include crystallography, NMR spectroscopy, or cryo-electron microscopy studies. The R497Q mutation allows scientists to explore what structural changes this specific amino acid swap causes in protein folding and overall shape. The dual tagging system makes protein purification and handling much easier during these structural investigations. When researchers compare results with normal PLAT, they may discover important structure-function relationships.
3. Antibody Development and Validation
Scientists can use this tagged PLAT variant as an antigen to create specific antibodies against human tissue-type plasminogen activator. The high purity level (over 85%) makes it appropriate for the immunization steps in antibody production. Both the Myc and His tags allow for easy detection and measurement during antibody screening and validation work. The R497Q variant might also help develop antibodies that target this specific mutation, or test whether existing antibodies react differently with various PLAT forms.
4. ELISA and Immunoassay Development
This dual-tagged protein can work as a standard or control in enzyme-linked immunosorbent assays designed to detect and measure PLAT levels. The His-tag allows researchers to attach it in a specific orientation on nickel-coated plates. The Myc-tag offers another detection approach using anti-Myc antibodies. Scientists can use this recombinant protein to create standard curves and check how well their immunoassays perform. The defined R497Q mutation makes it particularly useful for developing assays that can tell different PLAT variants apart.
(M1)-SDS.jpg)
