This recombinant Drosophila melanogaster Partner of bursicon protein is produced in a yeast expression system, which appears to provide high fidelity to the native form. The protein comes with an N-terminal 6xHis tag that makes purification and detection more straightforward. The product spans the full length of the mature protein—specifically amino acids 21 to 141—and reaches a purity of greater than 90% as determined by SDS-PAGE. It's intended for research use only.
The Partner of bursicon protein plays what seems to be a critical role in the post-molt hardening of the exoskeleton in Drosophila melanogaster. It works as a neuropeptide hormone, forming a heterodimer with bursicon, and appears to be involved in regulating cuticle sclerotization and wing expansion. This protein may prove pivotal in studies related to insect development and molting processes, potentially offering insights into endocrine signaling pathways.
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. Protein-Protein Interaction Studies
This recombinant pburs protein can help investigate its binding partners and interaction networks in Drosophila development and physiology. The N-terminal 6xHis tag allows for purification and immobilization in pull-down assays to identify novel interacting proteins from fly lysates. Co-immunoprecipitation experiments using anti-His antibodies might validate specific interactions and determine binding stoichiometry. Such studies could contribute to understanding the molecular mechanisms underlying pburs function in fruit fly biology.
2. Antibody Development and Validation
The purified recombinant pburs protein works well as an antigen for generating specific antibodies against this Drosophila protein. The high purity (>90%) likely ensures minimal cross-reactivity during immunization protocols in laboratory animals. Generated antibodies can be validated using the recombinant protein in Western blot, ELISA, and immunofluorescence applications. These research-grade antibodies would enable detection and localization studies of endogenous pburs in Drosophila tissues and cell lines.
3. Biochemical Characterization and Structural Studies
This recombinant protein provides material for detailed biochemical analysis. This includes determination of molecular weight, isoelectric point, and stability under various buffer conditions. The 6xHis tag makes purification easier for biophysical studies such as circular dichroism spectroscopy to analyze secondary structure content. Size exclusion chromatography can reveal oligomerization states and protein complex formation. These characterization studies would establish fundamental biochemical properties of the pburs protein for future research applications.
4. In Vitro Functional Assays
The recombinant pburs protein can be incorporated into cell-free assay systems to study its biochemical properties and potential enzymatic activities. Binding assays using the His-tagged protein may screen for small molecule ligands or cofactors that could modulate its function. The purified protein enables dose-response studies to establish concentration-dependent effects in various in vitro experimental systems. These approaches might help elucidate the molecular basis of pburs function in controlled laboratory conditions.
