Recombinant Escherichia coli Uncharacterized protein YcbX (ycbX) is produced in an E. coli expression system and is available as a full-length protein from amino acids 1 to 369. The protein carries an N-terminal GST tag, which makes purification and detection more straightforward. SDS-PAGE analysis shows purity levels exceeding 85%, making this product suitable for research applications. Functional ELISA has confirmed biological activity, demonstrating binding to immobilized ldcC with an EC50 of 40.54-47.97 μg/ml.
The YcbX protein from Escherichia coli remains largely mysterious—its exact biological functions haven't been fully worked out yet. What we do know is that it can bind specific molecules, which suggests it may play a role in various cellular processes. As research continues, understanding how YcbX binds and what it does could shed light on its contribution to bacterial physiology and its potential connections to broader biological 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 with LdcC
The binding activity between this recombinant YcbX protein and ldcC (lysine decarboxylase) offers a solid starting point for investigating how they interact. The functional ELISA data showing specific binding with an EC50 range of 40.54-47.97 μg/ml indicates measurable affinity that researchers can characterize further. This protein could help scientists study binding kinetics, determine dissociation constants, and map which domains are responsible for the YcbX-ldcC interaction. The N-terminal GST tag makes purification and immobilization for various binding assays relatively simple.
2. GST Pull-Down Assays for Identifying Binding Partners
That N-terminal GST tag makes this recombinant YcbX protein particularly useful for GST pull-down experiments to fish out potential binding partners from E. coli cell lysates. Since we already know it binds ldcC, this protein can act as bait to capture and identify other interacting proteins that might be involved in similar cellular pathways. The GST tag allows for straightforward immobilization on glutathione-sepharose beads and subsequent elution of protein complexes for mass spectrometry analysis. This approach may help researchers piece together the functional network surrounding the still-mysterious YcbX protein.
3. Biochemical Characterization of an Uncharacterized E. coli Protein
Since YcbX remains uncharacterized, this recombinant protein presents an opportunity for fundamental biochemical studies to figure out what it actually does in cells. The confirmed biological activity and binding capability suggest it likely plays a role in protein-protein interactions within E. coli. Researchers can put this protein to work in structural studies, enzymatic activity screening, and functional annotation experiments. The high purity (>85%) and full-length expression (1-369aa) should ensure the protein maintains its native folding and whatever biological functions it naturally has.
4. Development of Binding Assays and Screening Platforms
The established binding activity with ldcC and those defined EC50 values make this protein a good candidate for developing standardized binding assays. Researchers could use this recombinant YcbX protein to create ELISA-based screening platforms for identifying small molecules or other proteins that might interfere with or enhance the YcbX-ldcC interaction. Those reproducible binding parameters provide a useful baseline for assay development and validation. Platforms like these could prove valuable for studying metabolic pathways involving lysine decarboxylase and related enzymatic processes in bacterial systems.
5. Antibody Development and Validation
This recombinant YcbX protein could work well as an immunogen for generating specific antibodies against this uncharacterized E. coli protein. The high purity and full-length expression should ensure that antibodies will recognize the native protein in bacterial cells. Scientists can use the GST tag for antibody purification through affinity chromatography, while the confirmed biological activity validates that the recombinant protein appears to maintain proper folding. These antibodies would become valuable research tools for studying YcbX expression, localization, and function in E. coli under different growth conditions.
