Recombinant Human Desmoglein-3 (DSG3) is expressed in E.coli and covers the 70-499 amino acid region of the protein. The protein carries an N-terminal 6xHis-SUMO tag to help with purification, reaching a purity level greater than 90% as confirmed by SDS-PAGE analysis. This recombinant protein is designed for research use only and provides reliable quality for experimental work, though no specific endotoxin level is specified.
Desmoglein-3 appears to be a key component of desmosomes—specialized structures that help cells stick together in epithelial tissues. The protein seems particularly important for maintaining tissue integrity and cohesion, especially in skin and mucous membranes. Research into DSG3's function and interactions may prove valuable for studies on cell adhesion, tissue development, and related diseases.
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. Antibody Development and Validation Studies
This DSG3 fragment (aa 70-499) could work as an immunogen or antigen for creating monoclonal or polyclonal antibodies against human desmoglein-3. The N-terminal His-SUMO tag makes purification and immobilization easier for immunization protocols or screening assays. Scientists might find this protein useful for validating antibody specificity through ELISA, Western blot, or surface plasmon resonance assays. The high purity (>90%) likely minimizes cross-reactivity issues during antibody characterization studies.
2. Protein-Protein Interaction Studies
The His-SUMO tagged DSG3 fragment may work well in pull-down assays to identify and study binding partners or interacting proteins from cell lysates or purified protein libraries. The His tag allows for immobilization on nickel-affinity matrices, while the SUMO tag offers additional purification options and might improve protein stability. This setup could help researchers explore DSG3's molecular interactions within desmosomal complexes or other cellular pathways under controlled in vitro conditions.
3. Structural and Biophysical Characterization
This purified DSG3 fragment spanning amino acids 70-499 appears suitable for structural biology studies, including X-ray crystallography, NMR spectroscopy, or cryo-electron microscopy. The high purity level should support biophysical analyses such as dynamic light scattering, circular dichroism spectroscopy, or analytical ultracentrifugation to examine protein folding, stability, and oligomerization states. The defined expression region may allow for systematic structure-function relationship studies of specific DSG3 domains.
4. ELISA-Based Binding and Competition Assays
The His-SUMO tagged DSG3 protein can be attached to ELISA plates or biosensor surfaces for quantitative binding studies with potential ligands, other desmosomal proteins, or small molecule compounds. Researchers might run competition assays to determine binding affinities and specificities of various interacting molecules. The tag system likely helps with oriented immobilization and consistent protein presentation for reproducible binding measurements in high-throughput screening applications.
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