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.
1. In Vitro Enzyme Activity Characterization
This recombinant 1,3-beta-glucanosyltransferase can help establish and optimize enzyme activity assays for studying fungal cell wall biosynthesis. The purified protein allows controlled biochemical studies to determine substrate specificity, kinetic parameters, and optimal reaction conditions. The N-terminal His-tag makes purification and immobilization straightforward for repeated assays. Such studies would likely provide fundamental insights into the enzymatic mechanisms behind fungal cell wall construction.
2. Antifungal Drug Screening Platform
The recombinant gel4 protein serves as a potentially valuable target for screening antifungal compounds that may inhibit cell wall biosynthesis enzymes. Researchers can develop high-throughput screening assays using this purified enzyme to identify small molecules or natural products that interfere with its glucanosyltransferase activity. The standardized recombinant system appears to ensure reproducible results across different screening campaigns. This approach might help identify novel antifungal lead compounds targeting fungal cell wall synthesis pathways.
3. Antibody Development and Validation
The purified recombinant gel4 protein can serve as an immunogen for generating specific antibodies against this fungal enzyme. The His-tagged protein seems suitable for immunization protocols and subsequent antibody characterization through ELISA and Western blot analyses. These antibodies would likely prove valuable as research tools for studying gel4 expression patterns, cellular localization, and protein levels in fungal cultures. The recombinant protein also works as a positive control and standard for antibody-based detection methods.
4. Protein-Protein Interaction Studies
This recombinant enzyme can be used in pull-down assays and other interaction studies to identify cellular partners involved in fungal cell wall biosynthesis complexes. The N-terminal His-tag allows immobilization on metal affinity matrices for capturing potential binding partners from fungal cell extracts. Such studies might reveal the molecular networks and regulatory mechanisms governing cell wall synthesis in Aspergillus fumigatus. The purified protein also enables validation of identified interactions through direct binding assays.
5. Structural and Biophysical Analysis
The recombinant gel4 protein provides material for detailed structural studies including X-ray crystallography, NMR spectroscopy, or cryo-electron microscopy to understand the molecular architecture of this glucanosyltransferase. Biophysical characterization techniques such as dynamic light scattering, differential scanning calorimetry, and circular dichroism spectroscopy can be applied to study protein stability, folding, and conformational changes. The high purity level makes it suitable for these sensitive analytical techniques that require well-characterized protein samples.
