Recombinant Human Nuclear pore membrane glycoprotein 210 (NUP210) is produced in E. coli and covers the 28-238 amino acid region of the protein. The protein includes an N-terminal 6xHis-tag and achieves greater than 90% purity, as confirmed by SDS-PAGE analysis. This partial protein appears suitable for research applications that require high-purity recombinant proteins.
Nuclear pore membrane glycoprotein 210 (NUP210) plays a critical role in the structure and function of nuclear pore complexes, which regulate the transport of molecules between the nucleus and cytoplasm. It participates in essential cellular processes such as nucleocytoplasmic transport, contributing to the maintenance of cellular homeostasis and the regulation of gene expression. NUP210 has become a significant focus in studies exploring nuclear-cytoplasmic interactions.
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 NUP210 is a transmembrane glycoprotein that functions as a structural component of the nuclear pore complex. Its native structure requires integration into the nuclear membrane and extensive glycosylation. The E. coli expression system cannot replicate the eukaryotic membrane environment or perform necessary post-translational modifications (e.g., glycosylation). The expressed fragment (28-238aa) is a partial extracellular domain, which likely lacks the full conformational epitopes and disulfide bonds required for native folding. Therefore, this recombinant protein is highly unlikely to be correctly folded or functionally active.
1. Antibody Development and Validation
This recombinant fragment serves as a suitable immunogen for generating antibodies against linear epitopes of NUP210's extracellular domain. The His-tag facilitates purification and screening. However, antibodies may not recognize conformational epitopes on the native, glycosylated protein in cellular contexts.
2. Biochemical Characterization and Stability Studies
This is a priority application to assess the protein's physical properties. Techniques like SEC-MALS and CD spectroscopy can evaluate oligomeric state, stability, and secondary structure. However, results will reflect the misfolded E. coli product, not native NUP210 behavior.
3. His-Tag Based ELISA Development
The protein is suitable as a standard in ELISA assays for detecting anti-NUP210 antibodies or quantifying immunoreactivity. However, it cannot be used for functional interaction screens (e.g., ligand binding) due to likely misfolding.
Final Recommendation & Action Plan
This recombinant NUP210 fragment is unsuitable for functional studies due to E. coli's inability to replicate its complex folding requirements. Prioritize Application 2 (Biochemical Characterization) to define the protein's properties. Applications 1 and 3 (antibody development and ELISA standards) can proceed for immunological uses. Transmembrane protein interactions depend on precise tertiary structure and glycosylation, which E. coli cannot produce such protein.For functional insights, use NUP210 expressed in eukaryotic systems (e.g., mammalian cells) with proper glycosylation and membrane integration.
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