Recombinant Mouse Tripeptidyl-peptidase 2 (Tpp2) is produced using a baculovirus expression system and includes amino acids 44 to 264. This partial protein carries an N-terminal 10xHis-tag and a C-terminal Myc-tag, which makes purification and detection more straightforward. SDS-PAGE analysis shows the protein purity exceeds 85%, indicating it should work well as a research reagent.
Tripeptidyl-peptidase 2 (Tpp2) appears to be a key protease that breaks down oligopeptides inside cells. The protein likely plays an important role in protein turnover and seems to be involved in various cellular processes, including immune response regulation. As part of the proteasome-associated complex, Tpp2 may be crucial for maintaining cellular protein balance, which makes it particularly interesting for researchers studying cell biology and immunology.
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 mouse Tpp2 fragment (amino acids 44-264) could work in pull-down experiments to find potential binding partners or other interacting proteins. The N-terminal His-tag allows researchers to attach it to nickel-affinity resins, and the C-terminal Myc-tag helps detect and confirm the bait protein when studying complex formation. This partial construct might still contain important interaction domains that could be mapped by testing it against cellular lysates or purified protein collections.
2. Antibody Development and Validation
Researchers could use the recombinant Tpp2 fragment as an immunogen or screening antigen when developing antibodies specific to mouse Tpp2. The dual tagging system creates built-in positive controls for immunoassays - anti-His or anti-Myc antibodies can check protein integrity and loading. This partial construct may display epitopes that antibodies can access easily while avoiding potential problems with full-length protein folding or stability issues.
3. Structural and Biochemical Characterization
The specific 44-264aa region of mouse Tpp2 is suitable for analysis using biophysical methods like circular dichroism spectroscopy, dynamic light scattering, or analytical ultracentrifugation to study its folding properties and how it forms complexes with itself. The high purity (over 85%) and dual tags make protein quantification and handling easier for structural work. This fragment might represent a stable domain or functional unit that could reveal details about how the complete enzyme is organized.
4. Tag-Based Detection Assays
The combination of His and Myc tags opens up possibilities for creating sandwich-type detection assays or ELISA-based methods for research purposes. Anti-His antibodies could capture the protein while anti-Myc antibodies handle detection, or researchers could switch these roles depending on what works better for their specific setup. This strategy might prove useful for tracking protein stability, developing purification methods, or creating quantitative approaches for other Tpp2-related studies.
