Code | CSB-EP012534HU |
Abbreviation | Recombinant Human KRT19 protein |
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Size | US$256 |
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Recombinant Human Keratin, type I cytoskeletal 19 (KRT19) is expressed in E. coli and includes the complete protein sequence from amino acids 1 to 400. The protein carries an N-terminal 6xHis tag that helps with purification and detection steps. SDS-PAGE analysis shows purity levels above 85%. This product is intended for research use only, with endotoxin levels below detectable limits, making it suitable for various experimental work.
Keratin 19 appears to be a type I intermediate filament protein that's central to maintaining structural integrity in epithelial cells. The protein participates in cytoskeleton formation and has become a standard marker in cancer research, particularly because of its presence in epithelial tissues. Studies examining cell structure and cancer diagnostics often rely on understanding how KRT19 functions and what it interacts with.
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 recombinant KRT19 protein may serve as an effective immunogen for creating monoclonal or polyclonal antibodies that target human keratin 19. Since the protein spans the full length (1-400aa), it likely provides broad epitope coverage for antibody screening and characterization work. The N-terminal 6xHis tag makes purification straightforward and allows for immobilization in ELISA-based validation experiments. Scientists can test how specific their antibodies are, measure binding strength, and fine-tune detection methods.
2. Protein-Protein Interaction Studies
Pull-down assays can take advantage of the 6xHis-tagged KRT19 to find and study proteins that bind to it during cytoskeletal organization. The tag allows researchers to attach the protein to nickel-affinity matrices, which then capture interacting proteins from cell lysates or purified protein collections. This method helps reveal keratin 19's role in intermediate filament assembly and cellular structural networks. The high purity (>85%) should give reliable interaction data with less background noise.
3. Structural and Biochemical Characterization
This recombinant protein provides material for biophysical studies. Techniques like circular dichroism spectroscopy, dynamic light scattering, and analytical ultracentrifugation can examine how KRT19 folds and whether it forms larger complexes. Having the full-length construct means researchers can study the complete protein's structural features under different buffer conditions and temperatures. The protein's stability, tendency to clump together, and shape changes related to cytoskeletal function become accessible for investigation.
4. In Vitro Filament Assembly Assays
Purified KRT19 protein can help recreate intermediate filament formation in test tubes when mixed with the right type II keratins. These assembly studies let researchers look at how fast filaments form, what they look like, and how different factors might speed up or slow down the process. Working with the recombinant system gives controlled conditions to study keratin filament behavior without the complications that come with whole cells. This approach may reveal detailed mechanisms behind cytoskeletal assembly.
5. Epitope Mapping and Immunoassay Development
The full-length KRT19 protein works as a reference standard when developing and improving immunoassays that target keratin 19. Epitope mapping studies using protein digestion or peptide competition can identify where antibodies actually bind. The 6xHis tag gives researchers control over how the protein is presented in different assay formats, which helps when developing sandwich ELISAs, Western blot procedures, and other detection methods for research applications.
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