Recombinant Mouse Angiogenin-4 (Ang4) is produced in a yeast expression system and contains the full-length mature protein sequence, specifically amino acids 25-144. An N-terminal 6xHis-sumostar tag is included to make purification and detection more straightforward. SDS-PAGE analysis shows the product has greater than 90% purity, which appears to make it suitable for various research applications that need high-quality protein samples.
Angiogenin-4 (Ang4) is a protein that's involved in angiogenesis - the process where new blood vessels form. This process seems crucial in many normal body functions as well as disease states. Ang4 belongs to the ribonuclease A superfamily and likely plays a role in how cells respond to changes in their surrounding environment. Researchers are particularly interested in Ang4 when studying blood vessel development and the signaling pathways that control it.
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. In Vitro Ribonuclease Activity Characterization
This recombinant mouse Angiogenin-4 may be useful for studying its potential ribonuclease activity, since angiogenins are part of the RNase A superfamily. The N-terminal His-tag makes purification easier and allows the protein to be attached to surfaces for enzyme studies using different RNA substrates. Scientists can compare how mouse Ang4 behaves enzymatically compared to other angiogenin family members. This might help reveal how protein structure relates to function. The yeast expression system provides a more complex cellular environment for protein folding, which could help preserve the protein's natural enzymatic activity.
2. Protein-Protein Interaction Studies
The His-sumostar tag system makes pull-down experiments more feasible for finding proteins that might bind to mouse Angiogenin-4 in cell extracts or with purified proteins. The tag allows researchers to attach the protein to nickel-based columns while keeping it accessible for interaction studies. This approach could help reveal the molecular mechanisms behind how Ang4 functions in cells. Since the recombinant protein has high purity, binding specificity experiments should give more reliable results.
3. Antibody Development and Validation
This purified recombinant mouse Ang4 appears well-suited as an immunogen for creating antibodies that specifically recognize mouse Angiogenin-4. The mature protein region (25-144aa) represents what's found naturally in biological systems, so antibodies made against it should recognize the native protein. High purity levels suggest there will be minimal unwanted reactions with contaminants during immunization. Scientists can then test these antibodies using the same recombinant protein in ELISA, Western blots, and other immune-based assays.
4. Comparative Structural and Biochemical Analysis
Researchers might use this recombinant protein for structural studies - trying to grow crystals for X-ray analysis, NMR studies, or other methods to understand mouse Ang4's three-dimensional structure. Comparing it with other angiogenin family members could reveal which structural features are conserved across species and which have changed. Testing the protein's stability and folding behavior under different conditions (various buffers, temperatures) may provide insights into how it functions. Such studies could contribute to understanding how the angiogenin protein family evolved over time.
