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.
1. Protein-Protein Interaction Studies Using His-Tag Pull-Down Assays
Researchers can attach the N-terminal 6xHis-tagged COPS2 protein to nickel-affinity resins. This setup helps identify and characterize binding partners within the COP9 signalosome complex or other cellular networks. The approach allows systematic screening of potential interacting proteins from cell lysates or purified protein collections. Since this recombinant protein covers the full sequence (1-443aa), all possible binding domains should remain intact for interaction studies. Mass spectrometry analysis of the pulled-down complexes might reveal insights into how COPS2 functions within protein networks and signaling cascades.
2. Antibody Development and Validation
This recombinant COPS2 protein works well as an antigen for creating specific antibodies against human COPS2 in research settings. The full-length protein offers multiple epitopes for both monoclonal and polyclonal antibody production, which may increase the chances of getting high-affinity, specific antibodies. The 85% purity appears adequate for immunization protocols and follow-up antibody characterization through ELISA, Western blotting, and specificity testing. Researchers can then use these antibodies to detect native COPS2 across different cell types and tissues.
3. Biochemical Characterization and Stability Studies
The purified recombinant COPS2 protein enables investigation of its biochemical properties—thermal stability, pH tolerance, and buffer compatibility under different experimental conditions. Techniques like dynamic light scattering, differential scanning fluorimetry, and size exclusion chromatography could provide useful data about protein folding, aggregation patterns, and optimal storage conditions. These studies seem essential for developing standardized protocols for COPS2 handling in lab settings and understanding what structural requirements keep the protein intact.
4. In Vitro Reconstitution Experiments for COP9 Signalosome Complex Assembly
This full-length COPS2 protein can be mixed with other recombinant COP9 signalosome subunits to examine complex assembly mechanisms and subunit interactions under controlled in vitro conditions. The yeast expression system likely produces properly folded protein that retains native-like structural features needed for complex formation. Such reconstitution studies might reveal the step-by-step assembly process, pinpoint critical binding interfaces, and determine the minimum subunit requirements for stable complex formation.
