Recombinant Apis mellifera Major royal jelly protein 1 (MRJP1) is produced using a baculovirus expression system, which appears to ensure high-quality protein synthesis. The protein spans the full mature length from amino acids 20-432. It includes an N-terminal 10xHis-tag that makes purification and detection more straightforward. SDS-PAGE analysis confirms purity levels exceeding 85%, suggesting it's well-suited for various research applications.
Major royal jelly protein 1 (MRJP1) represents a key component of royal jelly - that remarkable secretion honeybees use to nourish their larvae and adult queens. The protein likely plays a crucial role in honeybee development and colony dynamics. Given MRJP1's biological functions and its apparent involvement in nutrition and development, it has become an important subject of study in entomology and related fields.
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 Using His-Tag Pull-Down Assays
The N-terminal 10xHis tag on this recombinant MRJP1 protein makes nickel-affinity based pull-down experiments possible for identifying potential binding partners. Researchers can immobilize the His-tagged MRJP1 on nickel-coated beads or columns, then incubate with cell lysates or purified protein libraries from honeybee tissues. This approach may help clarify the molecular interactions of MRJP1 within royal jelly formation pathways or honeybee developmental processes. The 85% purity level should be sufficient for these interaction studies, since contaminating proteins can typically be distinguished from specific binding partners through appropriate controls.
2. Antibody Development and Immunoassay Applications
This recombinant MRJP1 can serve as an immunogen for generating polyclonal or monoclonal antibodies specific to honeybee MRJP1. The full-length mature protein (20-432aa) provides what appears to be comprehensive epitope coverage for antibody production in laboratory animals. The His-tagged protein can then function as a positive control and standard in ELISA-based assays to characterize antibody specificity and binding kinetics. These antibodies might later be applied in research studying MRJP1 expression patterns, localization, or quantification in honeybee samples.
3. Biochemical Characterization and Stability Studies
The recombinant MRJP1 protein opens doors for systematic biochemical analysis. This includes thermal stability profiling, pH tolerance testing, and proteolytic susceptibility assays. Researchers can investigate how the protein behaves under various buffer conditions, salt concentrations, and temperature ranges to understand its biophysical properties. The baculovirus expression system typically produces proteins with proper folding, which makes this particularly suitable for studying the inherent stability characteristics of MRJP1. Such studies could provide insights into the protein's role in royal jelly preservation and optimal storage conditions.
4. Comparative Protein Analysis and Evolutionary Studies
This recombinant MRJP1 may serve as a reference standard for comparative studies with MRJP1 variants from different honeybee subspecies or related proteins from other social insects. Researchers can perform side-by-side biochemical comparisons, electrophoretic mobility analysis, and cross-reactivity studies using the standardized recombinant protein. Consistent production through baculovirus expression should ensure reproducible material for multi-laboratory collaborative studies investigating the evolution and functional divergence of major royal jelly proteins across Apis species.
