Recombinant Triticum monococcum Omega-gliadin is produced in E. coli and comes with an N-terminal GST tag, which makes purification and detection more straightforward. This protein represents a partial-length sequence covering the 1-28 amino acid region and reaches over 90% purity according to SDS-PAGE analysis. Such high purity levels appear to provide reliable performance for various research applications, particularly when endotoxin levels aren't a major concern.
Omega-gliadin from Triticum monococcum—a type of einkorn wheat—functions as a seed storage protein that primarily handles the nutritional storage of amino acids. It seems to play an important role in plant development and has drawn interest from researchers working on cereal crop improvement and gluten-related studies. Understanding its structure and function may contribute to advances in agricultural biotechnology and nutritional science.
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. Gluten Protein Fragment Interaction Studies
This N-terminal fragment (1-28aa) of omega-gliadin can help researchers investigate protein-protein interactions within gluten networks in vitro. The GST tag makes pull-down assays possible for identifying binding partners or studying how this specific N-terminal region might contribute to gluten protein assembly. Scientists can examine whether this short fragment retains any binding capacity with other gliadin subunits or glutenin proteins. The high purity (>90%) likely ensures reliable results in biochemical binding assays and surface plasmon resonance studies.
2. Antibody Development and Epitope Mapping
The recombinant omega-gliadin fragment works as an immunogen or screening antigen for developing antibodies specific to the N-terminal region of Triticum monococcum omega-gliadin. The GST tag makes purification and immobilization easier for ELISA-based antibody screening and characterization. This fragment can help determine whether the N-terminal 28 amino acids contain immunogenic epitopes that differ from other gliadin regions. Such antibodies would probably serve as valuable research tools for studying einkorn wheat protein composition and processing.
3. Comparative Wheat Species Protein Analysis
This einkorn wheat omega-gliadin fragment appears useful as a reference standard in comparative studies examining gliadin diversity across different wheat species. Researchers can perform cross-reactivity studies using this purified fragment against antibodies raised to modern wheat gliadins. The defined 28-amino acid sequence allows for precise comparison of N-terminal regions between ancient and modern wheat varieties. Studies like these may contribute to understanding wheat evolution and protein structural conservation.
4. GST-Tagged Protein Purification Method Development
The GST-tagged omega-gliadin fragment serves as a model protein for optimizing purification protocols for wheat storage proteins expressed in E. coli. Researchers can use this product to test different glutathione affinity chromatography conditions and buffer systems. The known purity level provides a benchmark for evaluating purification efficiency and developing scalable protocols. This application seems particularly valuable for laboratories planning to express and purify other wheat protein fragments or domains.
