Recombinant Human 26S proteasome non-ATPase regulatory subunit 11 (PSMD11) is produced in E. coli and includes an N-terminal GST tag that makes purification easier. The protein covers the complete mature sequence from amino acids 2 to 422. SDS-PAGE analysis confirms purity levels above 90%, making this product suitable for research applications where consistent results matter.
PSMD11 appears to be a key component of the 26S proteasome—the cellular machinery that breaks down ubiquitinated proteins. This regulatory subunit likely plays an important role in keeping protein levels balanced and controlling different cellular activities. Within the ubiquitin-proteasome pathway, PSMD11 is particularly relevant for studies examining protein breakdown, cell cycle control, and signaling networks.
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 PSMD11 is a component of the 26S proteasome regulatory particle that requires precise folding, proper integration into multi-subunit complexes, and specific tertiary structure for its functional activity. The mammalian cell expression system provides the correct eukaryotic folding environment. However, the large N-terminal GST tag (~26 kDa), while not larger than the PSMD11 protein itself (~47 kDa), constitutes a significant portion (~36%) of the fusion protein's mass. This large tag may sterically interfere with the protein's complex assembly interfaces and functional domains. Crucially, PSMD11's functionality is entirely dependent on its correct assembly with other subunits into the 19S regulatory particle. Expressing it alone, without its partner proteins, makes achieving functional bioactivity highly improbable.
1. Antibody Development and Validation
This application is highly suitable. Antibody development relies on antigenic sequence recognition. The full-length, mammalian-expressed protein provides proper folding and authentic epitopes for generating specific antibodies, despite the presence of the tag.
2. Biochemical Characterization and Structural Studies
Basic biophysical characterization can be performed, but the GST tag will dominate the physical properties and mask the intrinsic characteristics of PSMD11. Structural studies (e.g., crystallography) would be invalid for determining the native structure of PSMD11 within the proteasome complex.
3. GST-Tagged Protein Purification and Detection Assays
This application is technically feasible for developing purification and detection methods leveraging the GST tag. However, it is useful only for technical workflow development and does not provide insights into PSMD11 biology.
Final Recommendation & Action Plan
This GST-tagged PSMD11 expressed alone in mammalian cells is unsuitable for functional studies related to proteasome biology. The large tag and, more importantly, the absence of essential partner subunits preclude its integration into a functional complex. Applications 2 and 3 have severe limitations and will not yield insights into native PSMD11 function. Only Application 1 (antibody development) is highly reliable. For functional PSMD11 research, it is essential to study the protein in the context of the complete 19S regulatory particle, either by co-expressing multiple subunits or studying the endogenous complex.
