Recombinant Human SPRY domain-containing SOCS box protein 1 (SPSB1) is produced in E. coli and includes the complete sequence spanning 1-273 amino acids. The protein comes with an N-terminal 10xHis-tag and a C-terminal Myc-tag, which makes purification and detection more straightforward. Purity levels appear to exceed 85%, based on SDS-PAGE analysis. This product is designed strictly for research purposes and may provide consistent results in experimental settings.
SPSB1 belongs to the suppressor of cytokine signaling (SOCS) box protein family. This protein family is recognized for its role in regulating different signaling pathways. SPSB1 seems to interact with components of the ubiquitin-proteasome system, potentially affecting how proteins get degraded. Research suggests SPSB1 plays an important role in cellular signaling, which could make it a valuable tool for studying protein regulation and signaling dynamics.
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 SPSB1 is a SPRY domain-containing protein that functions as an adaptor in E3 ubiquitin ligase complexes. The protein requires precise folding of its SPRY domain for protein-protein interactions and proper SOCS box formation for ubiquitin ligase recruitment. The E. coli expression system cannot provide the eukaryotic folding environment and post-translational modifications that may be important for this protein's full functionality. While the protein may be soluble, the dual N-terminal 10xHis-tag and C-terminal Myc-tag may sterically interfere with functional domains.
1. Protein-Protein Interaction Studies Using Pull-Down Assays
This application carries a significant risk without proper folding validation. SPSB1 interactions with other E3 ligase components require the precise tertiary structure of the SPRY domain. If correctly folded (verified), the protein is suitable for identifying physiological binding partners. If misfolded/unverified, there is high risk of non-specific binding or interaction failure.
2. Antibody Development and Validation
This application is highly suitable as antibody development relies on antigenic sequence recognition. The full-length protein provides comprehensive epitope coverage for both linear and conformational antibody production.
3. Biochemical Characterization and Stability Studies
These studies are essential for determining folding status. If correctly folded (verified), characterization provides reliable data on structural stability. If misfolded/unverified, analysis yields physical property data for quality control.
4. In Vitro Binding Assays with Tagged Detection
This application requires proper folding validation. Functional binding assays depend on native protein conformation. If correctly folded (verified), the protein enables valid interaction studies. If misfolded/unverified, binding assays will yield misleading results.
Final Recommendation & Action Plan
The E. coli expression system has limitations for this eukaryotic protein, but the full-length construct provides a reasonable starting point for characterization. Begin with Application 3 (Biochemical Characterization) to assess folding quality through size-exclusion chromatography and circular dichroism spectroscopy. Validate functional competence if possible using known binding partners. Once proper folding is verified, proceed cautiously with Applications 1 and 4 for interaction studies. Application 2 (antibody development) can proceed immediately. If misfolding is detected, limit applications to antibody production and basic biophysical characterization. For reliable SPSB1 functional studies, consider mammalian expression systems that better support eukaryotic protein folding.
