Recombinant Mouse Parvalbumin alpha (Pvalb) gets expressed in E. coli and covers the full mature protein length, spanning amino acids 2-110. This product comes with dual tagging - an N-terminal 10xHis-tag paired with a C-terminal Myc-tag, which makes purification and detection more straightforward. The protein reaches greater than 90% purity, as confirmed by SDS-PAGE. This level of purity appears to make it well-suited for demanding research applications.
Parvalbumin alpha is a calcium-binding protein that's typically involved in regulating muscle relaxation and neuronal signaling. It seems to play an important role in calcium homeostasis and acts as a key component across various physiological pathways. Researchers often rely on its presence as a marker when investigating muscle and neuronal function, which likely makes it a useful tool in both basic and applied research.
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.
Based on the provided information, the recombinant mouse Pvalb is expressed in E. coli, a prokaryotic system that is generally suitable for producing small, stable proteins like parvalbumin. Parvalbumin is a calcium-binding protein with EF-hand motifs that require precise folding and metal ion coordination for functionality. While E. coli can often properly fold small soluble proteins, the presence of dual tags (N-terminal 10xHis and C-terminal Myc) may interfere with the native structure, particularly at the termini. The protein is full-length mature (2-110aa) with >90% purity, which is favorable. However, since activity is unverified and parvalbumin requires specific calcium-binding capability, the protein cannot be assumed to be correctly folded or bioactive without experimental validation of its calcium-binding properties.
1. Antibody Development and Validation
This application is appropriate. The recombinant Pvalb can serve as an effective immunogen for generating antibodies that recognize linear epitopes. The high purity and full-length sequence support antibody production. However, the dual tags may generate antibodies against non-native epitopes. If the protein is misfolded, antibodies may not recognize conformational epitopes of native parvalbumin. Validation against endogenous parvalbumin is recommended.
2. Protein-Protein Interaction Studies
The dual tags enable technical feasibility for pull-down assays, but this application requires caution. Parvalbumin's interactions are calcium-dependent and conformation-sensitive. If the recombinant mouse Pvalb is misfolded or has impaired calcium-binding, identified interactions may not be physiological. This application should only be pursued after confirming proper folding and calcium-binding functionality.
3. Biochemical Characterization and Calcium-Binding Studies
This application is valuable but highly dependent on correct folding. Basic biochemical studies are feasible, but calcium-binding assays require proper EF-hand motif formation. If the protein is misfolded, calcium affinity measurements will be invalid. These studies should include validation of proper folding through circular dichroism (to confirm expected α-helical content) before interpreting calcium-binding data.
4. ELISA Development and Quantitative Assays
This application is feasible but with limitations. The tags facilitate assay development, but if Pvalb is misfolded, quantitative measurements may not correlate with native protein levels. The assay may work for detection, but requires validation against properly folded parvalbumin to ensure accurate quantification.
Final Recommendation & Action Plan
Given the uncertainty in folding and bioactivity, recommend first performing biophysical and functional characterization. This should include circular dichroism spectroscopy to verify the expected α-helical content characteristic of parvalbumin's EF-hand motifs, and calcium-binding assays using isothermal titration calorimetry or fluorescence-based methods to confirm functionality. Antibody development can proceed as the safest application. Protein interaction studies and quantitative assays should await proper folding validation. For reliable calcium-binding studies, ensure the protein is properly refolded if necessary, and include calcium-free and calcium-saturated controls in experiments.
