Recombinant Phleum pratense Pollen allergen Phl p 5a is produced in E. coli with a partial protein length of 1-286 amino acids. The protein carries an N-terminal 10xHis-SUMO tag along with a C-terminal Myc tag, which helps with purification and detection processes. SDS-PAGE analysis shows the product achieves greater than 85% purity, suggesting it meets quality standards for research applications. This product is intended for research use only.
Phleum pratense Pollen allergen Phl p 5a appears to be a significant component when studying grass pollen allergies. As an allergenic protein, it likely plays a crucial role in immune responses that pollen exposure triggers. Research into Phl p 5a tends to focus on understanding how it interacts with the immune system. This work may contribute to developing allergy diagnostics and potential therapeutic interventions.
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. Allergen-Specific Antibody Development and Characterization
This recombinant Phl p 5a protein can work as an immunogen for generating monoclonal or polyclonal antibodies specific to timothy grass pollen allergens. The dual-tagged design with N-terminal His-SUMO and C-terminal Myc tags allows for efficient purification and detection during antibody screening. ELISA-based assays can leverage the Myc tag to identify high-affinity antibodies that specifically recognize the Phl p 5a allergen. These antibodies would likely prove valuable as research tools for studying allergen distribution, cross-reactivity patterns, and structural epitope mapping.
2. Protein-Protein Interaction Studies Using Pull-Down Assays
The N-terminal His tag makes it possible to immobilize the recombinant Phl p 5a protein on nickel-based affinity matrices for pull-down experiments. Researchers can incubate the immobilized protein with cell lysates or purified protein preparations to identify potential binding partners or interacting molecules. The C-terminal Myc tag offers an additional detection method to confirm protein integrity and loading in these interaction studies. This approach might reveal novel molecular interactions relevant to allergen function or processing pathways.
3. Structural and Biochemical Characterization Studies
The high purity level (>85%) and dual-tag system appear to make this protein suitable for detailed biochemical analysis and structural studies. The His tag allows for efficient purification protocols while the Myc tag works for protein detection and quantification in various analytical techniques. Researchers can subject the recombinant protein to biophysical characterization methods such as circular dichroism spectroscopy, dynamic light scattering, or analytical ultracentrifugation to study its folding properties and solution behavior. These studies would likely provide fundamental insights into the molecular properties of this timothy grass allergen.
4. Cross-Reactivity Analysis in Allergen Research
This recombinant Phl p 5a protein works as a standardized antigen for investigating cross-reactivity patterns between different grass pollen allergens in controlled laboratory settings. The consistent expression system and purification tags help ensure reproducible protein preparations for comparative binding studies. Competition assays or inhibition studies using this protein can examine how antibodies or other molecules interact with related allergens from different grass species. The Myc tag makes detection and quantification straightforward in multiplexed assay formats designed to study allergen cross-reactivity profiles.
