Recombinant Drosophila melanogaster GEO11329p1 (ITP) is produced in a mammalian cell expression system, which appears to ensure proper folding and post-translational modifications. The protein is expressed as the full length of its mature form, spanning amino acids 33 to 119, and carries a C-terminal hFc1 tag for easier detection and purification. The product achieves a purity of greater than 90%, as verified by SDS-PAGE analysis, making it suitable for various research applications.
GEO11329p1, also known as ITP, is a protein found in Drosophila melanogaster—the common fruit fly. It likely plays a crucial role in signaling pathways that are important for cellular communication and regulation. Scientists often study this protein for its involvement in key physiological processes, which has made it a significant focus in research related to insect biology and genetics.
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. Ion Transport Peptide (ITP) Functional Studies in Drosophila Research
This recombinant ITP protein can be used to investigate the physiological roles of ion transport peptides in Drosophila melanogaster through in vitro binding assays and receptor interaction studies. The mammalian cell expression system may ensure proper protein folding and post-translational modifications that could be critical for biological function. The C-terminal hFc1 tag simplifies protein detection and purification for biochemical characterization experiments. Researchers can use this protein to study ITP signaling pathways and their effects on ion homeostasis in fruit fly model systems.
2. Antibody Development and Validation
The high purity recombinant ITP protein serves as what appears to be an excellent immunogen for generating specific antibodies against Drosophila ITP. The C-terminal hFc1 tag allows for straightforward immobilization on protein A/G columns for antibody purification and validation assays. These antibodies can subsequently be used for immunohistochemistry, Western blotting, and other detection methods in Drosophila research. The mature protein region (33-119aa) represents the biologically relevant form, which suggests it would be ideal for producing antibodies that recognize native ITP in biological samples.
3. Protein-Protein Interaction Studies
The hFc1-tagged recombinant ITP can be used in pull-down assays to identify potential binding partners and interacting proteins in Drosophila protein extracts. The Fc tag enables efficient capture using protein A/G beads, which makes co-immunoprecipitation experiments more straightforward. This approach may help clarify the molecular mechanisms underlying ITP function and identify components of ITP signaling complexes. Mass spectrometry analysis of pulled-down complexes could reveal novel regulatory proteins involved in ion transport regulation.
4. ELISA-Based Quantitative Assays
The recombinant ITP protein can serve as a standard or capture reagent in enzyme-linked immunosorbent assays for measuring endogenous ITP levels in Drosophila tissue extracts or hemolymph samples. The C-terminal hFc1 tag provides a convenient handle for immobilization and detection in sandwich ELISA formats. This application would likely be valuable for studying ITP expression patterns during different developmental stages or under various physiological conditions. The high purity of the protein suggests it should provide reliable and reproducible quantitative measurements in comparative studies.
