Recombinant Neosartorya fumigata 1,3-beta-glucanosyltransferase gel4 is produced in a yeast expression system, delivering the full-length mature protein from amino acids 26 to 519. The protein includes an N-terminal 6xHis-tag, which streamlines purification and detection processes. SDS-PAGE analysis shows the protein achieves greater than 85% purity, suggesting reliable performance for various research applications. This product is intended strictly for research use only—not for diagnostic or therapeutic purposes.
1,3-beta-glucanosyltransferase gel4 from Neosartorya fumigata appears to play a crucial role in fungal cell wall biosynthesis. The enzyme seems particularly important in forming and remodeling beta-glucan polymers. Its activity may be vital for maintaining cell wall integrity, which makes it an attractive target for studying fungal growth and development. Understanding gel4's function could prove essential for research into antifungal strategies and broader fungal biology questions.
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.
Neosartorya fumigata 1,3-beta-glucanosyltransferase Gel4 is a fungal enzyme that requires precise folding, proper active site formation, and specific tertiary structure for its catalytic activity in cell wall biosynthesis. The yeast expression system is highly suitable for expressing fungal proteins as it provides a compatible eukaryotic folding environment, potential glycosylation, and disulfide bond formation. The N-terminal 6xHis-tag is relatively small and unlikely to cause significant steric interference. The expression of the full-length mature protein (26-519aa) in this system provides a high probability of correct folding with functional enzymatic activity, though experimental validation is still recommended.
1. In Vitro Enzyme Activity Characterization
This application is highly suitable. The yeast-expressed full-length enzyme has a high probability of being functionally active. The His-tag facilitates easy purification for kinetic studies (Km, Vmax) and substrate specificity assays. Activity should be validated using established glucanosyltransferase assays.
2. Antifungal Drug Screening Platform
This application is suitable provided enzyme activity is confirmed. The recombinant protein can serve as an excellent target for high-throughput screening of inhibitors. The yeast expression system likely produces a conformationally relevant target for identifying physiologically active compounds.
3. Antibody Development and Validation
This application is highly suitable. The full-length, properly folded protein expressed in a eukaryotic system presents authentic epitopes for generating high-quality antibodies specific to Gel4, useful for detection and localization studies in fungi.
4. Protein-Protein Interaction Studies
This application is suitable, with the caveat that interactions must be validated in the fungal context. The correctly folded protein can identify potential partners in cell wall biosynthesis complexes, but physiological relevance should be confirmed.
5. Structural and Biophysical Analysis
This application is highly suitable. The protein's high purity and likely correct folding make it appropriate for structural studies (X-ray, Cryo-EM) and biophysical characterization (DSC, CD) to understand its catalytic mechanism.
Final Recommendation & Action Plan
This yeast-expressed Gel4 with a small N-terminal His-tag is highly likely to be properly folded and functional due to the compatibility between the fungal protein and the yeast expression system. All proposed applications are suitable. Priority should be given to validating enzymatic activity (Application 1) as this confirms bioactivity fundamental to Applications 2 and 4. Applications 3 and 5 can proceed concurrently. This recombinant protein represents a well-suited tool for studying fungal cell wall biosynthesis and antifungal development.
