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.
Human DSG3 is a transmembrane cadherin-like protein that requires complex folding, including disulfide bond formation, calcium ion binding, and correct dimerization for bioactivity. E. coli, as a prokaryotic expression system, lacks the machinery for eukaryotic-specific post-translational modifications (e.g., glycosylation) and cannot properly fold transmembrane proteins or their extracellular domains. The partial length (aa 70-499) likely corresponds to the extracellular domain but misses the transmembrane and intracellular regions, which are critical for native conformation. The His-SUMO tag may improve solubility but can interfere with folding. Therefore, this protein is highly unlikely to be correctly folded or bioactive, as it probably forms misfolded aggregates or non-functional structures.
Given the high likelihood of misfolding, this recombinant DSG3 protein should not be used for functional studies (e.g., interactions or binding assays) without prior validation of its conformation. First, perform basic biophysical tests (e.g., circular dichroism to check for expected β-sheet structures, and size-exclusion chromatography to monitor oligomerization) to assess folding status. If misfolding is confirmed, limit applications to non-functional uses like antibody production.
This DSG3 fragment can be used as an immunogen for antibody production, as antibodies may recognize linear epitopes even in misfolded proteins. However, antibodies generated might not bind to native, correctly folded DSG3 in physiological contexts (e.g., in tissues or cell surfaces). The high purity reduces cross-reactivity risks, but validation must include testing against full-length, properly folded DSG3 from mammalian cells to ensure specificity. The His-SUMO tag could induce non-specific antibodies, so tag removal or control experiments are advised.
For reliable results, consider switching to a eukaryotic expression system (e.g., mammalian or insect cells) for producing full-length DSG3 with correct folding and activity.
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