Recombinant Synechocystis sp. Ribonuclease J comes from an E. coli expression system and contains the complete protein sequence covering amino acids 1-640. The protein includes an N-terminal 6xHis-SUMO tag, which makes purification and detection more straightforward. SDS-PAGE analysis confirms that purity exceeds 90%, ensuring researchers get high-quality samples. This product is designed strictly for research purposes and cannot be used for therapeutic or diagnostic applications.
Ribonuclease J appears to play a vital role in RNA metabolism, where it participates in both RNA maturation and degradation processes. The enzyme seems integral to maintaining RNA stability and proper cellular function. Scientists study Ribonuclease J to better understand RNA processing pathways, which may help reveal molecular mechanisms in prokaryotic organisms like Synechocystis sp. Research into its function could potentially offer valuable insights into basic biological processes and might even lead to biotechnological applications.
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.
Synechocystis sp. Ribonuclease J (rnj) is a complex bacterial enzyme that requires precise folding, proper active site formation, specific metal ion coordination (typically magnesium or manganese), and correct tertiary structure for its ribonuclease activity. The E. coli expression system is homologous to this bacterial enzyme, which increases the probability of correct folding. However, the large N-terminal 6xHis-SUMO tag (∼15 kDa) may sterically interfere with the protein's active site, substrate-binding domains, or oligomerization interfaces. While the full-length protein (1-640aa) contains all functional domains, the probability of correct folding with functional ribonuclease activity requires experimental validation of metal ion incorporation and catalytic competence.
1. In Vitro Ribonuclease Activity Characterization
This application carries a significant risk without functional validation. Ribonuclease J activity requires precise metal ion coordination, proper active site formation, and correct tertiary structure. If correctly folded and active (verified through RNA degradation assays), the protein may be suitable for kinetic studies. If misfolded/inactive (unverified), enzymatic measurements will yield biologically meaningless results. The SUMO tag may sterically interfere with RNA substrate access.
2. Comparative Enzymology Studies
Meaningful comparative studies require native enzyme conformation and functional activity. If correctly folded and active (verified), the protein enables valid evolutionary comparisons of ribonuclease properties. If misfolded/inactive (unverified), comparative analyses would yield misleading insights about enzyme conservation and divergence across bacterial species.
3. Protein-RNA Interaction Studies
This application requires proper folding validation. Ribonuclease J interactions with RNA substrates require precise tertiary structure and active site formation. If correctly folded (verified), the protein may identify physiological RNA interactions. If misfolded/unverified, there is a high risk of non-specific binding or failure to replicate genuine RNA-enzyme interactions.
4. Antibody Development and Validation
This application is highly suitable as antibody development relies on antigenic sequence recognition rather than functional enzymatic activity. The full-length protein provides comprehensive epitope coverage for generating rnj-specific antibodies. The high purity (>90%) ensures minimal contamination-related issues during immunization protocols.
5. Biochemical Inhibitor Screening
This application carries a high risk without functional validation. Inhibitor screening requires native enzyme conformation and catalytic activity. If correctly folded and active (verified), limited screening may be possible. If misfolded/inactive (unverified), screening results will be unreliable for identifying genuine enzyme inhibitors.
Final Recommendation & Action Plan
The E. coli expression system is favorable for producing this bacterial ribonuclease J due to homologous expression conditions, but the large SUMO tag necessitates experimental validation before functional applications. Begin with metal content analysis and ribonuclease activity assays using RNA substrates to confirm functionality. Applications 1, 2, 3, and 5 require rigorous functional validation before proceeding. Application 4 (antibody development) can proceed immediately. For reliable ribonuclease research, consider SUMO tag removal for critical kinetic and inhibitor studies to minimize potential steric interference with the active site and RNA-binding domains.
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