Recombinant Pongo abelii Transmembrane protein 168 (TMEM168) is expressed in E. coli, covering the amino acid region 527-637. This partial protein product features an N-terminal 10xHis-tag and a C-terminal Myc-tag for enhanced purification and detection. The protein shows a purity greater than 85%, as confirmed through SDS-PAGE analysis, which appears to ensure reliable results in experimental applications.
TMEM168 likely plays a role in cellular processes involving membrane dynamics and signaling. As a transmembrane protein, it seems to be implicated in various pathways related to cellular communication and structural integrity. Understanding TMEM168's function may be crucial for research in membrane biology and related fields, potentially offering insights into cell signaling and structural maintenance.
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 Pull-Down Assays
The dual-tagged TMEM168 protein fragment (N-terminal His-tag and C-terminal Myc-tag) provides versatile options for investigating potential protein interactions. The His-tag enables immobilization on nickel-based resins for pull-down experiments with cell lysates or purified protein libraries. Meanwhile, the Myc-tag allows for detection and validation of interactions through Western blotting or immunoprecipitation approaches. This partial protein fragment (527-637aa) may retain key interaction domains that could reveal novel binding partners in primate cellular pathways.
2. Antibody Development and Epitope Mapping
This recombinant TMEM168 fragment can serve as an immunogen for generating specific antibodies against Pongo abelii TMEM168 or related primate orthologs. The 111-amino acid fragment appears to provide sufficient antigenic material for immunization protocols in laboratory animals. The dual tags help with purification and quality control during antibody production, while also enabling competitive binding assays to map epitope locations. Generated antibodies could prove valuable for studying TMEM168 expression and localization in primate tissue samples or cell culture systems.
3. Structural and Biophysical Characterization Studies
The purified TMEM168 fragment offers opportunities for detailed structural analysis using techniques such as circular dichroism spectroscopy, dynamic light scattering, and potentially NMR or crystallography studies. The high purity level (>85%) and defined boundaries (527-637aa) make this fragment suitable for investigating the folding properties and stability of this specific TMEM168 domain. Comparative structural studies between this Pongo abelii fragment and corresponding regions from other primate species could provide insights into evolutionary conservation and structural features.
4. Cross-Species Comparative Biochemical Analysis
This Pongo abelii TMEM168 fragment enables comparative studies with human and other primate TMEM168 orthologs to investigate species-specific differences in protein properties. The defined expression region (527-637aa) allows for production of equivalent fragments from other species for direct biochemical comparisons. Such studies might examine differences in protein stability, solubility, or interaction profiles between species. The dual-tag system provides consistent purification and detection methods across different species variants for standardized comparative analysis.
