Recombinant Human COP9 signalosome complex subunit 2 (COPS2) comes from a yeast expression system and spans the complete 443 amino acid protein. The construct includes an N-terminal 6xHis-tag for easier purification and detection. SDS-PAGE analysis shows this product reaches purity levels above 85%. It's intended solely for research purposes and appears to offer a dependable resource for studying protein-protein interactions and related investigations.
COPS2 belongs to the COP9 signalosome, a multi-protein assembly that participates in diverse cellular processes—protein degradation and signal transduction among them. The protein seems to play an important role in controlling the ubiquitin-proteasome pathway, which likely contributes to how cells manage protein stability and activity. Getting a handle on COPS2's function may be key to understanding cellular regulation and homeostasis mechanisms.
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.
Human COPS2 is a component of the multiprotein COP9 signalosome complex that requires precise folding and proper integration into the complex for its functional role in protein degradation regulation. The yeast expression system provides a eukaryotic environment that supports proper protein folding and post-translational modifications, increasing the probability of correct folding compared to bacterial systems. However, as a complex subunit, COPS2's full functional activity depends on proper assembly with other COP9 subunits. The N-terminal 6xHis tag is relatively small but may potentially interfere with complex formation interfaces. While yeast expression provides favorable conditions, experimental validation remains essential to confirm structural integrity and complex assembly capability.
1. Protein-Protein Interaction Studies Using His-Tag Pull-Down Assays
This application is highly dependent on proper folding validation. COPS2 interactions within the COP9 signalosome require precise tertiary structure. If correctly folded (verified), the protein is suitable for identifying physiological interaction partners with other COP9 subunits. If misfolded/unverified, there is a high risk of non-specific binding or failure to identify genuine complex interactions.
2. Antibody Development and Validation
Antibody development relies primarily on antigenic sequence recognition. If correctly folded (verified), the protein excels for generating conformation-sensitive antibodies that recognize native COPS2 epitopes. If misfolded/unverified, it remains suitable for producing antibodies against linear epitopes, which are still valuable for detection applications.
3. Biochemical Characterization and Stability Studies
These studies are essential for determining folding status regardless of functional state. If correctly folded (verified), characterization provides reliable data on oligomerization, stability, and structural properties. If misfolded/unverified, analysis yields valuable physical property data for this specific preparation.
4. In Vitro Reconstitution Experiments for COP9 Signalosome Complex Assembly
This application requires rigorous folding and functional validation. Complex assembly depends on precise protein-protein interactions. If correctly folded (verified), the protein enables valid reconstitution studies with other COP9 subunits. If misfolded/unverified, assembly experiments will yield misleading results about complex formation mechanisms.
Final Recommendation & Action Plan
The yeast expression system provides favorable folding conditions for this COP9 signalosome subunit, but experimental validation of structural integrity and complex assembly capability is essential before reliable use in functional studies. Begin with Application 3 (Biochemical Characterization) to assess folding quality through size-exclusion chromatography (oligomerization state), circular dichroism spectroscopy, and thermal stability assays. If correct folding is verified, proceed to validate functional activity through complex assembly assays with other COP9 subunits. Once folding and assembly capabilities are confirmed, proceed cautiously with Applications 1 and 4 for interaction studies and complex reconstitution. Application 2 (antibody development) can proceed immediately regardless of folding status. If misfolding is detected, limit applications to linear epitope antibody production and basic biophysical characterization, avoiding all functional interaction and complex assembly studies. For reliable COPS2 research, always include appropriate complex assembly controls and consider using co-expression systems for complete COP9 signalosome studies.
