Recombinant Enterobacteria phage T4 Recombination protein uvsY is produced in E. coli with an N-terminal MBP-tag and a C-terminal 6xHis-Avi-tag, which makes detection and purification more straightforward. The protein expresses as a full-length version spanning amino acids 1-137. SDS-PAGE analysis confirms purity levels greater than 85%. This biotinylated protein appears suitable for various research applications, though it's designated for research use only.
The uvsY protein from Enterobacteria phage T4 acts as a recombination mediator protein. It seems to play a crucial role in homologous recombination by helping pair homologous DNA strands. During presynaptic filament assembly, it works alongside other recombination proteins. Scientists studying DNA repair mechanisms and the molecular processes behind genetic exchange in phage biology may find this protein particularly valuable.
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.
Enterobacteria phage T4 Recombination protein UvsY is a small (137 aa) protein that requires precise folding, proper oligomerization (hexamer formation), and specific tertiary structure for its functional activity in DNA recombination. The E. coli expression system is homologous to this phage protein, which increases the probability of correct folding at the domain level. However, the large N-terminal MBP tag (∼40 kDa) is significantly larger than the UvsY protein itself (∼15 kDa) and will severely sterically interfere with the protein's oligomerization interfaces and functional domains. While the protein may be correctly folded at the primary structure level, the probability of forming functional oligomers with proper bioactivity is extremely low due to the massive tag interference.
1. Antibody Development
This application has significant limitations. While antibodies can be generated against linear epitopes, the immune response will primarily target the large foreign MBP tag rather than the small UvsY domain. Antibodies may not recognize the native, properly oligomerized UvsY in its physiological context, and will likely have poor specificity for the actual functional protein.
2. Biophysical Characterization
Basic biophysical analysis can be performed, but will not reflect native UvsY structure or oligomerization. Techniques like circular dichroism spectroscopy or dynamic light scattering will primarily detect the large MBP tag's properties rather than the UvsY domain's characteristics. The tag will dominate all physical measurements, making results biologically irrelevant for understanding native UvsY biophysics.
Final Recommendation & Action Plan
This MBP-tagged UvsY construct is unsuitable for meaningful biophysical characterization due to the severe steric interference from the massive MBP tag (40 kDa) relative to the small UvsY protein (15 kDa). While antibody development is technically possible, the resulting antibodies will primarily recognize the tag rather than the native protein. For reliable UvsY research, use tag-free or small-tag constructs that preserve the protein's oligomerization capability and functional interfaces. Biophysical studies should be conducted with properly folded, untagged protein to obtain biologically relevant data.
