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 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.
1. Protein-Protein Interaction Studies Using His-Tag Pull-Down Assays
The N-terminal 6xHis-tagged NUP210 fragment (28-238aa) can be immobilized on nickel-affinity resins to identify and characterize potential binding partners within the nuclear pore complex or other cellular proteins. This partial sequence may contain important interaction domains that are likely involved in nucleocytoplasmic transport or nuclear envelope organization. The His-tag allows for efficient purification and immobilization for pull-down experiments with cell lysates or purified protein libraries. Such studies could help map the protein interaction network involving this specific region of NUP210.
2. Antibody Development and Validation
The recombinant NUP210 fragment with >90% purity can serve as an antigen for generating specific antibodies against the 28-238aa region of human NUP210. Researchers can use the purified protein for immunizing animals or screening hybridoma clones to develop monoclonal antibodies. It can also function as a positive control in antibody validation experiments such as Western blotting, ELISA, or immunoprecipitation assays. The His-tag also allows for easy detection and quantification during antibody characterization studies.
3. Biochemical Characterization and Stability Studies
The purified NUP210 fragment can be subjected to various biochemical analyses to determine its biophysical properties, including thermal stability, pH tolerance, and aggregation behavior under different buffer conditions. Techniques such as dynamic light scattering, differential scanning fluorimetry, or analytical ultracentrifugation may provide insights into the protein's folding state and stability profile. These studies appear essential for understanding the structural properties of this nuclear pore component and optimizing conditions for further experimental applications.
4. His-Tag Based ELISA Development
The N-terminal His-tag makes possible the development of sandwich or direct ELISA assays for detecting and quantifying NUP210 interactions or for screening compound libraries. The protein can be immobilized on nickel-coated plates or detected using anti-His antibodies in various ELISA formats. This approach seems particularly useful for high-throughput screening of small molecules or other proteins that may interact with the 28-238aa region of NUP210. The >90% purity should ensure reliable and reproducible results in quantitative assay development.
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