Recombinant Mouse Zinc finger protein 346 (Znf346) is produced in E.coli and includes the complete expression region spanning amino acids 1-294. The protein carries an N-terminal 6xHis-SUMO tag, which appears to improve both purification efficiency and overall stability. SDS-PAGE analysis confirms purity levels exceeding 90%, making it well-suited for detailed research applications. This product is designed exclusively for research purposes and should not be used for human or clinical applications.
Zinc finger protein 346 (Znf346) belongs to the zinc finger protein family, a group recognized for their DNA binding capabilities and roles in transcription regulation. Znf346 participates in several cellular processes, including gene expression control and RNA binding, which may explain its growing importance in studies focused on gene regulation and cellular signaling networks. This protein seems particularly useful for researchers trying to understand how transcriptional control actually works.
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-SUMO tag makes purification and immobilization of recombinant mouse Znf346 relatively straightforward for pull-down experiments. Researchers can use this zinc finger protein as bait to fish out potential binding partners from mouse cell lysates or purified protein collections. The >90% purity level should reduce background noise from contaminating proteins that might interfere with interaction studies. Since this is the full-length construct (1-294aa), it likely preserves all the protein interaction domains that could be important for normal cellular binding events.
2. Antibody Development and Validation
High purity recombinant mouse Znf346 may serve as a solid immunogen for creating specific antibodies against this zinc finger protein. The complete protein offers numerous epitopes for both monoclonal and polyclonal antibody generation. Researchers can then use the purified protein to test antibody specificity through ELISA, Western blot, and immunoprecipitation techniques. The His-SUMO tag simplifies purification and makes it easier to quantify the antigen for consistent immunization procedures.
3. Biochemical Characterization and Stability Studies
Purified recombinant protein opens the door for thorough biochemical analysis, including molecular weight determination, isoelectric point measurement, and thermal stability profiling. Scientists might use circular dichroism spectroscopy to examine the secondary structure and folding patterns of the zinc finger domains. Testing the protein under different buffer conditions and pH ranges could help establish the best storage and experimental parameters. These fundamental studies provide the groundwork needed for developing more sophisticated assays later.
4. In Vitro Binding Assays with Nucleic Acids
Since Znf346 is a zinc finger protein, recombinant mouse Znf346 could prove useful in electrophoretic mobility shift assays (EMSA) to explore possible DNA or RNA binding properties. The purified protein allows researchers to systematically test how well it binds to different nucleic acid sequences or structures. Surface plasmon resonance or fluorescence polarization techniques can measure binding kinetics and thermodynamics with greater precision. The His-SUMO tag helps with protein immobilization for biosensor-based binding experiments while keeping the protein intact.
