Recombinant Rat Trypsin-4 (Try4) is produced in E. coli and contains the full length of the mature protein, covering amino acids 24 to 247. With an N-terminal 6xHis-tag, this protein is purified to over 85% as determined by SDS-PAGE analysis. It's designed strictly for research use, offering what appears to be a dependable tool for various biochemical applications.
Trypsin-4 is a serine protease that plays a role in protein digestion. Part of the trypsin family, it seems to be critical for catalyzing the hydrolysis of peptide bonds, which breaks down proteins. Scientists frequently study this enzyme for its role in protein processing, and it's become essential in research examining proteolytic pathways and digestive enzyme function.
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 Using Pull-Down Assays
The N-terminal 6xHis-tagged recombinant rat trypsin-4 can be attached to nickel-affinity resins to find potential binding partners or substrates in rat tissue lysates or cell extracts. This method may allow researchers to explore the molecular interactions of Try4 across different biological settings. The high purity (>85%) likely reduces background binding from contaminating proteins during pull-down experiments. These studies could reveal insights into cellular pathways and regulatory networks that involve rat trypsin-4.
2. Antibody Development and Validation
This recombinant protein works well as an antigen for creating specific antibodies against rat trypsin-4, both polyclonal and monoclonal types. Since the full-length mature protein (24-247aa) includes the complete antigenic profile, antibodies should recognize native rat Try4 in different research settings. Scientists can use this protein for antibody screening, specificity testing, and measuring binding strength through ELISA-based assays. The His-tag makes purification and attachment straightforward for antibody validation work.
3. Structural and Biochemical Characterization Studies
Recombinant rat trypsin-4 can be used for detailed structural analysis using methods like X-ray crystallography, NMR spectroscopy, or cryo-electron microscopy. Scientists can examine the three-dimensional structure, folding patterns, and shape changes of this serine protease family member. High purity levels make it suitable for biophysical studies including thermal stability analysis, circular dichroism spectroscopy, and dynamic light scattering experiments. Such work might help explain the molecular basis of Try4 function and its evolutionary development.
4. Comparative Proteomics and Species-Specific Studies
This rat-specific trypsin-4 protein makes possible comparative studies with trypsin relatives from other species to explore evolutionary relationships and functional differences. Researchers can conduct cross-species binding studies, compare substrate preferences, and perform genetic analyses using this well-defined recombinant protein. The E. coli expression system appears to provide consistent protein production for larger comparative experiments. Research like this could advance our understanding of trypsin family evolution and how digestive enzymes have adapted differently across species.
