Recombinant E. coli tnaa protein

TNAA recombinant protein is a engineered protein derived through genetic recombination technology, designed to study or modulate specific biological processes. While "TNAA" isn't a widely standardized acronym in public databases, it likely refers to a protein associated with targeted cellular functions—potentially linked to tumor suppression, neurodegenerative pathways, or apoptosis regulation, given naming conventions in biomedical research. Such recombinant proteins are typically produced by inserting codon-optimized DNA sequences into expression systems (e.g., E. coli, yeast, or mammalian cells), followed by purification via affinity chromatography.

The protein often includes fusion tags (e.g., His-tag, GST) for isolation and detection. Its structural integrity is validated through SDS-PAGE, Western blot, and functional assays like ELISA or cell-based activity tests. TNAA recombinant protein may serve as a critical tool in drug discovery, particularly for screening inhibitors/activators in disease-relevant pathways. In translational research, it could be used to investigate protein-protein interactions, signal transduction mechanisms, or as an antigen for antibody development.

Applications extend to disease models, where exogenous TNAA supplementation might rescue phenotypic abnormalities or enhance therapeutic outcomes. Quality control ensures endotoxin levels <0.1 EU/μg for in vivo studies. As with most recombinant proteins, batch-to-batch consistency and proper storage (-80°C in stabilizer buffers) are essential to maintain bioactivity. Researchers utilize TNAA recombinant protein to dissect molecular pathways with higher specificity than synthetic compounds, accelerating mechanistic studies in personalized medicine and target validation.